CA2454572A1 - Crystalline pde4d2 catalytic domain complex, and methods for making and employing same - Google Patents

Abstract

The presently disclosed subject matter provides a crystalline form of a substantially pure phosphodiesterase 4D2 (PDE4D2) polypeptide. Also provided is a crystalline form of a substantially pure phosphodiesterase 4D2 (PDE4D2) polypeptide in complex with a ligand. Also provided are methods for generating the crystalline forms of the presently disclosed subject matter and methods for identifying and designing phosphodiesterase ligands and modulators. Also provided are scalable three-dimensional configurations of points and computer readable storage media containing digitally encoded structural data.

Description

--- DEyIANDES OU BRE'VE'TS VOLUVIINEUX
LA PRESENTE PARTIE DE CETTE DEi~LW\TDE OU CE BREVETS
COyIPREND PLUS D'UN TOME.
CECI EST LE TO1~IE ~ DE c~Z
NOTE: Pour les tomes additionels, veillez contactar 1e Bureau Canadien des Brevets.
JUMBO APPLICATIONS / PATENTS
THIS SECTION OF THE APPLICA T llOi~i I PATE~i T CON T AiNS i'i~iv~r~tE
THE1.N ONE VOLUIYIE.
THIS IS VOLUME I, OF
NOTE: For additional volumes please contact the Canadian Patent Office.

CRYSTALLINE PDE4D2 CATALYTIC DOMAIN COMPLEX.
AND METHODS FOR MAKING AND EMPLOYING SAME
Grant Statement This work was supported by grant GM59791 from the U.S. National 5 Institutes of Health (NIH). Thus, the U.S. government has certain rights in the presently disclosed subject matter.
Cross-Reference to Related Application This application is based on and claims priority to United States Provisional Patent Application Serial Number 60/444,640, filed February 3, 2003, herein incorporated by reference in its entirety.
Technical Field The presently disclosed subject matter relates generally to the structures of the PDE4D2 catalytic domain, and more particularly to crystal structures of an unliganded PDE4D2 catalytic domain and a PDE4D2 1s catalytic domain in complex with a ligand. The presently disclosed subject matter also relates to PDE4D2 catalytic domain binding compounds and to the design of compounds that bind to the PDE4D2 catalytic domain.
Abbreviations A - Angstrom 2o AMP - adenosine monophosphate ATCC - American Type Culture Collection cAMP - cyclic 3',5' adenosine monophosphate CaMV - cauliflower mosaic virus CCDC - Cambridge Crystallographic Data Center 2s CD - catalytic domairi cDNA - complementary DNA

cGMP - cyclic 3',5' guanosine monophosphate CNS - Crystallography and NMR System CPU - central processing unit so CRT - cathode ray tube DMSO - dimethyl sulfoxide DNA - deoxyribonucleic acid EST - expressed sequence tag FEDs - field emission displays GMP - guanosine monophosphate HEPES - N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic s acid Kd - dissaciatian constant kD - kilodalton(s) LCDs - liquid crystal displays LED - light emitting diade ~o MIR - multiple isomorphous replacement MPD - methyl pentanediol nt - nucleotides) PCR - polymerase chain reaction PDE - phosphodiesterase 15 PDE4D2 - phosphodiesterase 4D2 PEG - polyethylene glycol p1 - isoelectric point RAM - random access memory RUBISCO ribulose bisphosphate carboxylase -2o SIRAS - single isomorphous replacement with anomalous scattering TMV - tobacco mosaic virus Amino Acid Codes, Abbreviations. and Functionally Eauivalent Codons Amino Acid3-Letter 1-Letter Codons 2s Alanine Ala A GCA GCC GCG GCU

Arginine Arg R AGA AGG CGA CGC CGG CGU

AsparagineAsn N AAC AAU

Aspartic D GAC GAU
Acid Asp Cysteine Cys C UGC UGU

3o Glutamic E GAA GAG
acid Glu Glutamine Gln Q CAA CAG

Glycine Gly G GGA GGC GGG GGU

Histidine His H CAC .CAU

2 Isoleucine Ile I AUA AUC AUU

Leucine Leu L UUA UUG CUA CUC CUG CUU

Lysine Lys K AAA AAG

Methionine Met M AUG

s PhenylalaninePhe F UUC tJUU

Proline Pro P CCA CCC CCG CCU

Serine Ser S ACG AGU UCA UCC UCG UCU

Threonine Thr T ACA ACC ACG ACU

Tryptophan Trp W UGG
~o Tyrosine Tyr Y UAC UAU
Valine Val V GUA GUC GUG GUU
Background /art Cyclic 3',5'-adenosine and guanosine monophosphates (CAMP and cGMP, respectively) are intracellular second messengers that mediate the response of cells to a wide variety of stimuli, primarily through the activation of cyclic nucleotide activated protein kinases. Regulation of cAMP and cGMP concentrations in vivo is essential for many metabolic processes, such as cardiac and smooth muscle contraction, glycogenolysis, platelet aggregation, secretion, lipolysis, ion channel conductance, apoptosis, growth 2o control, and neurological function (reviewed by Houslay 1998; Antoni, 2000;
Lucas et al., 2000; Klein, 2002; Stork and Schimitt, 2002; Mehats et al., 2002). Cyclic nucleotide phosphodiesterases (PDEs) are enzymes hydrolyzing cAMP and/or cGMP to adenosine monophosphate (AMP) and/or guanosine monophosphate (GMP) and are essential for the regulation of 2s cyclic nucleotide concentrations in the cell (Torphy, 1998; Conti and Jin, 1999; Soderling and Beavo, 2000).
The human genome encodes twenty-one PDE genes categorized into 11 families (Thompson, 1991; Manganiello et al., 1995; Muller et al., 1996;
Houslay and Milligan, 1997; Zhao et al., 1997; Houslay et al., 1998; Torphy so 1998; Corbin and Francis, 1999; Soderling and Beavo, 2000; Francis et al, 2001; Mehats et aL, 2002;). Additional diversity is generated through the alternate splicing of PDE mRNAs, producing over 60 PDE isoforms in various human tissues. Family-selective inhibitors of PDEs constitute a

3 rapidly growing class of pharmaceuticals directed against several diseases and are widely studied as cardiotonic agents, vasodilators, smooth muscle relaxants, anti-depressants, anti-thrombotic compounds, anti-asthma compounds, and agents for improving cognitive functions such as memory s (Corbin and Francis, 2002; Giembycz, 2000, 2002; Huang et al., 2001; Reilly and Mohler, 2001; Rotella, 2002; Souness et al., 2000; Spina, 2003). For example, the PDES inhibitor sildenafil (VIAGRA~) is a drug for male erectile dysfunction and the PDE3 inhibitor cilostamide is a drug for heart diseases.
Selective inhibitors of PDE4 form the largest group of inhibitors for any PDE
~o family, and have been studied as anti-inflammatory drugs targeting asthma and chronic obstructive pulmonary disease (Piaz and Giovannoni, 2000;
Barnette and Underwood, 2000; Giembycz, 2002; Sturton and Fitzgerald, 2002).
All PDE enzymes share 25% sequence homology throughout a ~5 conserved catalytic domain of approximately 300 amino acids, suggesting that diverse PDE enzymes share a conserved active site structure and enzymatic mechanism. However, each PDE family recognizes a specific substrate and possesses its own selective inhibitors. The families PDE4, 7, and 8 prefer to hydrolyze cAMP while PDES, 6, and 9 are cGMP specific.
2o PDE1, 2, 3, 10, and 11 can hydrolyze both cAMP and cGMP.
To date, it is not known how the similar catalytic pockets of the different PDE families distinguish CAMP from cGMP and what the mechanism of hydrolysis is. The presently disclosed subject matter addresses these and other needs in the art.
2s Summary The presently disclosed subject matter provides a crystalline form comprising a substantially pure phosphodiesterase 4D2 (PDE4D2) polypeptide. In one embodiment; the presently disclosed subject matter provides a crystalline form comprising a substantially pure so phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide in complex with a ligand. In one embodiment, the crystalline form has unit cell a = 99.2 A; b = 111.2 A; c = 159.7 A. In another embodiment, the crystalline form has a space group of P2~2~2~. In another embodiment, the crystalline form

4 comprises four phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptides. In another embodiment, the crystalline form is such that the three-dimensional structure of the crystallized complex can be determined to a resolution of about 2.3 A or better. In another embodiment of the presently

5 disclosed subject matter, the phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide has the amino acid sequence shown in SEQ ID N0:4.
In yet another embodiment, the complex has a crystalline structure further characterized by the coordinates corresponding to one of Table 4 and Table 5.
The presently disclosed subject matter also provides methods of generating a crystalline form comprising a phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide in complex with a ligand, the method comprising: (a) incubating a solution comprising a phosphodiesterase 4D2 (PDE4D2) catalytic domain and a ligand; and (b) crystallizing the 15 phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide and ligand by vapor difFusion, whereby a crystalline form of a phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide in complex with a ligand is generated. In another embodiment, the crystalline form is grown by vapor diffusion against a well buffer comprising 50 mM HEPES (pH 7.5), 15%
2o PEG3350, 25% ethylene glycol, 5% methanol, and 5% DMSO. In another embodiment, the crystalline form is grown at 4°C. In another embodiment, the ligand is CAMP. In one embodiment, the solution comprises 10 mM
cAMP, 0.4 mM zinc sulfate, 15 mg/mL phosphodiesterase 4D2 (PDE4D2) in a storage buffer of 50 mM NaCI, 20 mM Tris-HCI (pH 7.5), and 1 mM f3-2s mercaptoethanol. In still another embodiment, the method further comprises saturating cAMP binding by soaking the crystalline form in a buffer of 50 mM
HEPES (pH 7.5), 20°lo PEG3350, 25% ethylene glycol, 0.4 mM zinc sulfate, and 50 mM cAMP. In one embodiment, the saturating occurs at room temperature.
3o The presently disclosed subject matter also provides a crystalline form formed by the methods of the presently disclosed subject matter.
The presently disclosed subject matter also provides a binding site in a human phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide for a substrate, wherein the substrate is in van der Waals, hydrogen bonding, or both van der Waals and hydrogen bonding contact with at least one of the following residues of the human phosphodiesterase 4D2 (PDE4D2) polypeptide: Tyr159, His160, His164, His200, Asp201, Met273, .Asp318, s Leu319, Asn321, Thr333, I1e336, Phe340, GIn369, and Phe372. In one embodiment, the binding site comprises four phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptides. In another- embodiment, at least two of the four phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptides are in van der Waals, hydrogen bonding, or both van der Waals ~o and hydrogen bonding contact through at least one of the following residues:
Arg116, Met147, Thr148, Asp151, Asn214, Thr215, Asn216, GIu218, AIa220, Leu221, Met222, Tyr223, Asn224, Asp225, Asn231, Leu234, A1a235, Lys239, GIn24,2, GIu243, GIu244, Lys254, Arg257, GIn258, Arg261, I1e265, Arg346, GIu349, and Arg350. In another embodiment, the binding ~s site further comprises a metal ion.
The presently disclosed subject matter also provides a complex of a human phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide and a substrate, wherein the substrate is in van der Waals, hydrogen bonding, or both van der Waals and hydrogen bonding contact with at least one of the 2o following residues of the human phosphodiesterase 4D2 (PDE4D2) polypeptide: Tyr159, His160, His164, His200, Asp201, Met273, Asp318, Leu319, Asn321, Thr333, I1e336, Phe340, GIn369, and Phe372. In one embodiment, the complex comprises four phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptides. In another embodiment, at least two of the z5 four phosphodiesterase 4D2 (PDE4D2) catalytic domain poiypeptides are in van der Waals, hydrogen bonding, or both van der Waal and hydrogen bonding contact through one or more of the following residues: Arg116, Met147, Thr148, Asp151, Asn214, Thr215, Asn216, GIu218, AIa220, Leu221, Met222, Tyr223, Asn224, Asp225, Asn231, Leu234, A1a235, 3o Lys239, GIn242, GIu243, GIu244, Lys254, Arg257, GIn258, Arg261, I1e265, Arg346, GIu349, and Arg350. In still another embodiment, the complex further comprises a metal ion.

6 The presently disclosed subject matter also provides a crystal of a complex of a human phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide and a substrate. In one embodiment, the crystal has the following physical measurements: space group P2~2,2~; and unit cell a =
5 99.2A;b=111.2 A;c=159.7 A.
The presently disclosed subject matter also provides a method for identifying a phosphodiesterase ligand, the method comprising: (a) providing atomic coordinates of a phosphodiesterase 4D2 (PDE4D2} catalytic domain in complex with a ligand to a computerized modeling system; and (b) modeling a ligand that fits spatially into the binding site of the phosphodiesterase 4D2 (PDE4D2) catalytic domain to thereby identify a phosphodiesterase ligand. In one embodiment, the phosphodiesterase 4D2 (PDE4D2) catalytic domain comprises the amino acid sequence of SEQ ID
N0:4. In another embodiment, the method further comprises identifying in ~s an assay for phosphodiesterase-mediated activity a modeled ligand that increases or decreases the activity of the phosphodiesterase.
The presently disclosed subject matter also provides a method of identifying a phosphodiesterase 4D2 (PDE4D2) ligand that selectively binds a phosphodiesterase 4D2 (PDE4D2) polypeptide compared to other 2o polypeptides, the method comprising: (a) providing atomic coordinates of a phosphodiesterase 4D2 (PDE4D2) catalytic domain in complex with a ligand to a computerized modeling system; and (b) modeling a ligand that fits into the binding pocket of a phosphodiesterase 4D2 (PDE4D2) catalytic domain and that interacts with residues of a phosphodiesterase 4D2 (PDE4D2) 25 catalytic domain that are conserved among phosphodiesterase 4D2 (PDE4D2) subtypes to thereby identify a phosphodiesterase 4D2 (PDE4D2) ligand that selectively binds a phosphodiesterase 4D2 (PDE4D2) polypeptide compared to other polypeptides. In one embodiment, the phosphodiesterase 4D2 (PDE4D2) catalytic domain comprises the amino so acid sequence shown in SEQ lD N0:4. In another embodiment, the method further comprises identifying in a bialogical assay for phosphodiesterase 4D2 (PDE4D2) activity a modeled ligand that selectively binds to said

7 phosphodiesterase 4D2 (PDE4D2) and increases or decreases the activity of the phosphodiesterase 4D2 (PDE4D2).
The presently disclosed subject matter also provides a method for designing a ligand of a phosphodiesterase 4D2 (PDE4D2) polypeptide, the s method comprising: (a) forming a complex of a compound bound to the phosphodiesterase 4D2 {PDE4D2) polypeptide; (b) determining a structural feature of the .complex formed in (a); wherein the structural feature is of a binding site for the compound; and (c) using the structural feature determined in (b) to design a ligand of a phosphodiesterase 4D2 (PDE4D2) ~o polypeptide capable of binding to the binding site of the presently disclosed subject matter. fn one embodiment, the method further comprises using a computer-based model of the complex formed in (a) in designing the ligand.
The presently disclosed subject matter also provides a method of designing a ligand of a phosphodiesterase polypeptide, the method ~s comprising: (a) selecting a candidate phosphodiesterase ligand; (b) determining which amino acid or amino acids of a phosphodiesterase polypeptide interact with the ligand using a three-dimensional model of a crystallized protein, the model comprising a phosphodiesterase 4D2 (PDE4D2) catalytic domain in complex with a ligand; (c) identifying in a 2o biological assay for phosphodiesterase activity a degree to which the ligand modulates the activity of the phosphodiesterase polypeptide; (d) selecting a chemical modification of the ligand wherein the interaction between the amino acids of the phosphodiesterase polypeptide and the ligand is predicted to be modulated by the chemical modification; (e) synthesizing a 25 ligand having the chemical modified to form a modified figand; (f) contacting the modified ligand with the phosphodiesterase polypeptide; (g) identifying in a biological assay for phosphodiesterase activity a degree to which the modified ligand modulates the biological activity of the phosphodiesterase polypeptide; and' (h) comparing the biological activity of the 30 phosphodiesterase polypeptide in the presence of modified ligand with the biological activity of the phosphodiesterase polypeptide in the presence of the unmodified ligand, whereby a ligand of a phosphodiesterase polypeptide is designed. In one embodiment, the phosphodiesterase is

8 phosphodiesterase 4D2 (PDE4D2). In another embodiment, the phosphodiesterase 4D2 (PDE4D2) polypeptide is a human phosphodiesterase 4D2 {PDE4D2) polypeptide. In another embodiment, the phosphodiesterase 4D2 (PDE4D2) polypeptide comprises the amino acid s sequence of SEQ ID N0:4. In another embodiment, the method further comprises repeating steps (a) through (f), if the biological activity of the phosphodiesterase polypeptide in the presence of the modified ligand varies from the biological activity of the phosphodiesterase polypeptide in the presence of the unmodified ligand.
~o The presently disclosed subject matter also provides a method of designing a chemical compound that modulates the biological activity of a target phosphodiesterase polypeptide, the method comprising: (a) obtaining three-dimensional structures for a catalytic domain (CD) of .
phosphodiesterase 4D2 (PDE4D2) bound to a figand, wherein the structures ~s are selected from the group consisting of X-ray structures and computer generated models; (b) rotating and translating the three-dimensional structures as rigid bodies so as to superimpose corresponding backbone atoms of a core region of the phosphodiesterase 4D2 (PDE4D2) CD; (c) comparing the superimposed three-dimensional structures to identify volume 2o near a catalytic pocket of the PDE CD that is available to a ligand in one or more structures, but not available to the ligand in one or more other structures; (d) designing a chemical compound that could occupy the volume in some of the complexed structures, but not in others; (e) synthesizing the designed chemical compound; and (f) testing the designed chemical 25 compound in a biological assay to determine whether it acts as a ligand of a phosphodiesterase with a desired effect on phosphodiesterase biological activities, whereby a ligand of a phosphodiesterase polypeptide is designed.
In one embodiment, the method further comprises designing a chemical compound by considering a known ligand of the PDE CD and adding a so substituent that protrudes into the volume identified in step (c) or that makes a desired interaction. In another embodiment, the phosphodiesterase is PDE4D2. In another embodiment, the designing a chemical compound further comprises using computer modeling software.

9 The presently disclosed subject matter also provides a method of designing a ligand that selectively modulates the activity of a phosphodiesterase polypeptide, the method comprising: (a) evaluating a three-dimensional structure of a crystallized phosphodiesterase 4D2 s (PDE4D2) catalytic domain polypeptide in complex with a ligand; and (b) synthesizing a potential ligand based on the three-dimensional structure of the crystallized phosphodiesterase 4D2 (PDE4D2) catalytic polypeptide in complex with a ligand, whereby a ligand that selectively modulates the activity of a phosphodiesterase polypeptide is designed. In one embodiment, the phosphodiesterase is phosphodiesterase 4D2 (PDE4D2).
In another embodiment, the phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide comprises the amino acid sequence of SEQ 1D N0:4. In another embodiment, the crystallized phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide is in an orthorhombic crystalline form. In another embodiment, the three-dimensional structure of the crystallized phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide in complex with a ligand can be determined to a resolution of about 2.3 A or better. In another embodiment, the method further comprises contacting a phosphodiesterase catalytic domain polypeptide with the potential ligand and 2o a ligand; and assaying the phosphodiesterase catalytic domain polypeptide for binding of the potential ligand, for a change in activity of the phosphodiesterase catalytic domain polypeptide, or both.
The presently disclosed subject matter also provides a method of screening a plurality of compounds for a ligand of a phosphodiesterase 4D2 25 (PDE4D2) catalytic domain polypeptide, the method comprising: (a) providing a library of test samples; {b) contacting a crystalline form comprising a phosphodiesterase 4D2 (PDE4D2) polypeptide in complex with a ligand with each test sample; (c) detecting an interaction between a test sample and the crystalline phosphodiesterase 4D2 (PDE4D2) polypeptide in so complex with a ligand; (d) identifying a test sample that interacts with the crystalline phosphodiesterase 4D2 (PDE4D2) polypeptide in complex with a ligand; and (e) isolating a test sample that interacts with the crystalline phosphodiesterase 4D2 (PDE4D2) polypeptide in complex with a ligand, whereby a plurality of compounds is screened for a ligand of a phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide. In one embodiment, the phosphodiesterase 4D2 (PDE4D2) polypeptide comprises a phosphodiesterase 4D2 (PDE4D2) catalytic domain. In another 5 embodiment, the phosphodiesterase 4D2 (PDE4D2) polypeptide is a human phosphodiesterase 4D2 (PDE4D2} polypeptide. In another embodiment, the phosphodiesterase 4D2 (PDE4D2) polypeptide comprises the amino acid sequence of SEQ ID N0:4. In another embodiment, the library of test samples is bound to a substrate. In still another embodiment, the library of ~o test samples is synthesized directly on a substrate.
The presently disclosed subject matter also provides a crystallized, recombinant polypeptide comprising: (a) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (b) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 ~s or SEQ ID NO: 4; or (c) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID
NO: 3 and has at least one biological activity of PDE4D2; wherein the polypeptide of (a}, (b} or (c) is in crystal form. In one embodiment, the 2o complex is in crystal form. In another embodiment, the complex is in crystal form. In another embodiment, the crystallized, recombinant polypeptide diffracts x-rays to a resolution of about 3.5 A or better. In another embodiment, the polypeptide comprises at least one heavy atom label. In another embodiment, the polypeptide is labeled with seleno-methionine.
25 The presently disclosed subject matter also provides a method for designing a modulator for the prevention or treatment of a disease or disorder, comprising: (a) providing a three-dimensional structure for a crystallized, recombinant polypeptide of claim 1; (b) identifying a potential modulator for the prevention or treatment of a disease or disorder by 3o reference to the three-dimensional structure; (c) contacting a polypeptide of the composition of claim 1 or a phosphodiesterase (PDE) with the potential modulator; and (d) assaying the activity of the polypeptide after contact with the modulator, wherein a change in the activity of the polypeptide indicates that the modulator may be useful for prevention or treatment of a disease or disorder.
The presently disclosed subject matter also provides a method for obtaining structural information of a crystallized polypeptide, the method s comprising: (a) crystallizing a .recombinant polypeptide, wherein the polypeptide comprises: (1 ) an amino acid sequence set forth in SEQ ID NO:
2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95%
identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID
NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that ~o hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID NO: 3 and has at least one biological activity of human PDE4D2; and wherein the crystallized polypeptide is capable of diffracting X-rays to a resolution of 3.5 A or better;
and (b) analyzing the crystallized polypeptide by X-ray diffraction to 15 determine the three-dimensional structure of at least a portion of the crystallized polypeptide. In one embodiment, the three-dimensional structure of the portion of the crystallized polypeptide is determined to a resolution of 3.5 A or better.
The presently disclosed subject matter also provides a method for 2o identifying a druggable region of a polypeptide, the method comprising: (a) obtaining crystals of a polypeptide comprising (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence encoded by 2s a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID
NO: 3 and has at least one biological activity of human PDE4D2, such that the three dimensional structure of the crystallized polypeptide may be determined to a resolution of 3.5 A or better; (b) determining the three so dimensional structure of the crystallized polypeptide using X-ray diffraction;
and (c) identifying a druggable region of the crystallized polypeptide based on the three-dimensional structure of the crystallized polypeptide. In one embodiment, the druggable region is an active site. In another embodiment, the druggable region is on the surface of the polypeptide.
The presently disclosed subject matter also provides a crystallized polypeptide comprising (1) an amino acid sequence set forth in SEQ ID NO:
5 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95%
identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID
NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID NO: 3 and has at least one biological activity of human PDE4D2; wherein the crystal has a P2~2~2~
space group.
The presently disclosed subject matter also provides a crystallized polypeptide comprising a structure of a polypeptide that is defined by a substantial portion of the atomic coordinates set forth in Table 4 or Table 5.
~5 The presently disclosed subject matter also provides a method for determining the crystal structure of a homolog of a polypeptide, the method comprising: (a) providing the three dimensional structure of a first crystallized polypeptide comprising (1 ) an amino acid sequence set forth in SEQ ID NO:
2 or SEQ ID NO: 4; (2) an amino acid sequence having at (east about 95%
2o identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID
NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID NO: 3 and has at least one biological activity of human PDE4D2; (b) obtaining crystals of a second 25 polypeptide comprising an amino acid sequence that is at least 70°1° identical to the amino acid sequence set forth in SECT ID NO: 2 or SEQ ID NO: 4, such that the three dimensional structure of the second crystallized polypeptide may be determined to a resolution of 3.5 A or better; and (c) determining the three dimensional structure of the second crystallized 3o polypeptide by x-ray crystallography based on the atomic coordinates of the three dimensional structure provided in step (a). In one embodiment, the atomic coordinates for the second crystallized polypeptide have a root mean square deviation from the backbone atoms of the first polypeptide of not more than 1.5 A for all backbone atoms shared in common with the first polypeptide and the second polypeptide.
The presently disclosed subject matter also provides a method for homology modeling a homofog of human PDE4D2, comprising: (a) aligning s the amino acid sequence of a homolog of human PDE4D2 with an amino acid sequence of SEQ ID NO: 2 or SEQ ID NO: 4 and incorporating the sequence of the homolog of human PDE4D2 into a model of human PDE4D2 derived from structure coordinates as listed in Table 4 or Table 5 to yield a preliminary model of the hamolog of human PDE4D2; (b) subjecting the preliminary model to energy minimization to yield an energy minimized model; (c) remodeling regions of the energy minimized model where stereochemistry restraints are violated to yield a final model of the homolog of human PDE4D2.
The presently disclosed subject matter also provides a method for ~s obtaining structural information about a molecule or a molecular complex of unknown structure comprising: (a) crystallizing the molecule or molecular complex; (b) generating an x-ray diffraction pattern from the crystallized molecule or molecular complex; and (c) applying at least a portion of the structure coordinates set forth in Table 4 or Table 5 to the x-ray diffraction 2o pattern to generate a three-dimensional electron density map of at least a portion of the molecule or molecular complex whose structure is unknown.
The presently disclosed subject matter also provides a method for attempting to make a crystallized complex comprising a polypeptide and a modulator having a molecular weight of less than 5 kDa, the method 2s comprising: (a) crystallizing a polypeptide comprising (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the 3o complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID
NO: 3 and has at least one biological activity of human PDE4D2; such that crystals of the crystallized polypeptide will diffract x-rays to a resolution of 5 A or better; and (b~ soaking the crystals in a solution comprising a potential modulator having a molecular weight of less than 5 kDa.
The presently disclosed subject matter also provides a method for incorporating a potential modulator in a crystal of a polypeptide, comprising s placing a hexagonal crystal of human PDE4D2 having unit cell dimensions a = 99.2 A; b = 111.2 k; c = 159.7 A, a = ~i = y = 9a°, with an orthorhombic space group P2~2~2~, in a solution comprising the potential modulator.
The presently disclosed subject matter also provides a computer readable storage medium comprising digitally encoded structural data, wherein the data comprises structural coordinates as listed in Table 4 or Table 5 for the backbone atoms of at least about six amino acid residues from a druggable region of human PDE4D2.
The presently disclosed subject matter also provides a scalable three-dimensional configuration of points, at least a portion of the points derived ~5 from some or all of the structure coordinates as listed in Table 4 or Table far a plurality of amino said residues from a druggable region of human PDE4D2. In one embodiment, the structure coordinates as listed in Table 4 or Table 5 for the backbone atoms of at least about five amino acid residues from a druggable region of human PDE4D2 are used to derive part or all of 2o the portion of points. In another embodiment, the structure coordinates as listed in Table 4 or Table 5 for the backbone and optionally the side chain atoms of at least about ten amino acid residues from a druggable region of human PDE4D2 are used to derive part or all of the portion of paints. In another embodiment, the structure coordinates as listed in Table 4 or Table 2s 5 for the backbone atoms of at least about fifteen amino acid residues from a druggable region of human PDE4D2 are used to derive part or all of the portion of points: In another embodiment, substantially all of the points are derived from structure coordinates as listed in Table 4 or Table 5. In still another embodiment, the structure coordinates as listed in Table 4 or Table 30 5 for the atoms of the amino acid residues from any of the above-described druggable regions of human PDE4D2 are used to derive part or all of the portion of points.

The presently disclosed subject matter also provides a scalable three-dimensional configuration of points, comprising points having a root mean square deviation of less than about 1.5 ~ from the three dimensional coordinates as listed in Table 4 or Table 5 for the backbone atoms of at least five amino acid residues, wherein the five amino acid residues are from a druggable region of human PDE4D2. In one embodiment, any point-to-point distance, calculated from the three dimensional coordinates as listed in Table 4 or Table 5, between one of the backbone atoms for one of the five amino acid residues and another backbone atom of a different one of the five amino acid residues is not more than about 10 A_ The presently disclosed subject matter also provides a scalable three-dimensional configuration of points comprising points having a root mean square deviation of less than about 1.5 A from the three dimensional coordinates as listed in Table 4 or Table 5 for the atoms of the amino acid ~5 residues from any of the above-described druggable regions of human PDE4D2.
The presently disclosed subject matter also provides a computer readable storage medium comprising digitally encoded structural data, wherein the data comprise the identity and three-dimensional coordinates as 20 listed in Table 4 or Table 5 for the atoms of the amino acid residues from any of the above-described druggable regions of human PDE4D2.
The presently disclosed subject matter also provides a scalable three-dimensional configuration of points, wherein the points have a root mean square deviation of less than about 1.5 A from the three dimensional 25 coordinates as listed in Table 4 or Table 5 for the atoms of the amino acid residues from any of the above-described druggable regions of human PDE4D2, wherein up to one amino acid residue in each of the regions may have a conservative substitution thereof.
The presently disclosed subject matter also provides a scalable three-3o dimensional configuration of points derived from a druggable region of a polypeptide, wherein the points have a root mean square deviation of less than about 1.5 A from the three dimensional coordinates as listed in Table 4 or Table 5 for the backbone atoms of at least ten amino acid residues that participate in the intersubunit contacts of human PDE4D2.
The presently disclosed subject matter also provides a computer-assisted method for identifying an inhibitor of the activity of human PDE4D2, 5 comprising: (a) supplying a computer modeling application with a set of structure coordinates as listed in Table 4 or Table 5 for the atoms of the amino acid residues from any of the above-described druggable regions of human PDE4D2 so as to define part or all of a molecule or complex; (b) supplying the computer modeling application with a set of structure coordinates of a chemical entity; and (c) determining whether the chemical entity is expected to bind to or interfere with the molecule or complex. In one embodiment, determining whether the chemical entity is expected to bind to or interfere with the molecule or complex comprises performing a fitting operation between the chemical entity and a druggable region of the 15 molecule or complex, followed by.computationally analyzing the results of the fitting operation to quantify the association between the chemical entity and the druggable region. In another embodiment, the method further comprises screening a library of chemical entities.
The presently disclosed subject matter also provides a computer-2o assisted method for designing an inhibitor of PDE4D2 activity comprising:
(a) supplying a computer modeling application with a set of structure coordinates having a root mean square deviation of less than about 1.5 A
from the structure coordinates as listed in Table 4 or Table 5 for the atoms of the amino acid residues from any of the above-described druggable regions 25 of human PDE4D2 so as to define part or all of a molecule or complex; (b) supplying the computer modeling application with a set of structure coordinates for a chemical entity; (c) evaluating the potential binding interactions between the chemical entity and the molecule or complex; (d) structurally modifying the chemical entity to yield a set of structure 3o coordinates for a modified chemical entity; and (e) determining whether the modified chemical entity is an inhibitor expected to bind to or interfere with the molecule or complex, wherein binding to or interfering with the molecule or molecular complex is indicative of potential inhibition of PDE4D2 activity.

In one embodiment, determining whether the modified chemical entity is an inhibitor expected to bind to or interfere with the molecule or complex comprises performing a fitting operation between the chemical entity and the molecule or complex, followed by computationally analyzing the results of s the fitting operation to evaluate the association between the chemical entity and the molecule or complex. In another embodiment, the set of structure coordinates for the chemical entity is obtained from a chemical library.
The presently disclosed subject matter also provides a computer-assisted method for designing an inhibitor of PDE4D2 activity de novo comprising: (a) supplying a computer modeling application with a set of three-dimensional coordinates derived from the structure coordinates as listed in Table 4 or Table 5 for the atoms of the amino acid residues from any of the above-described druggable regions of human PDE4D2 so as to define part or all of a molecule or complex; (b) computationally building a chemical 15 entity represented by a set of structure coordinates; and (c) determining whether the chemical entity is an inhibitor expected to bind to or interfere with the molecule or complex, wherein binding to or interfering with the molecule or complex is indicative of potential inhibition of PDE4D2 activity.
In one embodiment, determining whether the chemical entity is an inhibitor 2o expected to bind to or interfere with the molecule or complex comprises performing a fitting operation between the chemical entity and a druggable region of the molecule or complex, followed by computationally analyzing the results of the fitting operation to quantify the association between the chemical entity and the druggable region. In one embodiment, the method 2s further comprises supplying or synthesizing the potential inhibitor, then assaying the potential inhibitor to determine whether it inhibits PDE4D2 activity.
The presently disclosed subject matter also provides a method for identifying a potential modulator for the prevention or treatment of a disease 30 or disorder, the method comprising: (a) providing the three dimensional structure of a crystallized polypeptide comprising: (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence encoded by a polynucfeotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID
NO: 3 and has at least one biological activity of human PDE4D2; (b) s obtaining a potential modulator for the prevention or treatment of a disease or disorder based on the three dimensional structure of the crystallized polypeptide; (c) contacting the potential modulator with a second polypeptide comprising: (i) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID
NO: 4; (ii) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (iii) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ fD NO: 1 or SEQ ID NO: 3 and has at least one biological activity of human PDE4D2; which second polypeptide may optionally be the same as ~5 the crystallized poiypeptide; and (d) assaying the activity of the second polypeptide, wherein a change in the activity of the second polypeptide indicates that the compound may be useful for prevention or treatment of a disease or disorder.
The presently disclosed subject matter also provides a method for 2o designing a candidate modulator for screening for inhibitors of a polypeptide, the method comprising: (a) providing the three dimensional structure of a druggable region of a polypeptide comprising (1 ) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in 25 SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID
NO: 3 and has at least one biological activity of human PDE4D2; and (b) designing a candidate modulator based on the three dimensional structure of 3o the druggable region of the polypeptide.
The presently disclosed subject matter also provides a method for identifying a potential modulator of a polypeptide from a database, the method comprising: (a) providing the three-dimensional coordinates for a plurality of the amino acids of a polypeptide comprising (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence s encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID
NO: 3 and has at least one biological activity of human PDE4D2; (b) identifying a druggable region of the polypeptide; and (c) selecting from a database at least one potential modulator comprising three dimensional coordinates which indicate that the modulator may bind or interfere with the druggable region. In one embodiment, the modulator is a small molecule.
The presently disclosed subject matter also provides a method for preparing a potential modulator of a druggable region contained in a polypeptide, the method comprising: (a) using the atomic coordinates for the 15 backbone atoms of at least about six amino acid residues from a polypeptide of SEQ ID NO: 4, with a ~ a root mean square deviation from the backbone atoms of the amino acid residues of not more than 1.5 A, to generate one or more three-dimensional structures of a molecule comprising a druggable region from the polypeptide; (b) employing one or more of the three 2o dimensional structures of the molecule to design or select a potential modulator of the druggable region; and (c) synthesizing or obtaining the modulator.
The presently disclosed subject matter also provides an apparatus for determining whether a compound is a potential modulator of a polypeptide, 2s the apparatus comprising: (a) a memory that comprises: (i) the three dimensional coordinates and identities of at least about fifteen atoms from a druggable region of a polypeptide comprising (1) an amino acid sequence set forth ,in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in so SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ iD NO: 1 or SEQ ID
NO: 3 and has at least one biological activity of human PDE4D2; (ii) executable instructions; and (b} a processor that is capable of executing instructions to: (i) receive three-dimensional structural information for a candidate modulator; (ii) determine if the three-dimensional structure of the candidate modulator is complementary to the three dimensional coordinates of the atoms from the druggable region; and (iii) output the results of the determination.
The presently disclosed subject matter also provides a method for making an inhibitor of PDE4D2 activity, the method comprising chemically or enzymatically synthesizing a chemical entity to yield an inhibitor of PDE4D2 activity, the chemical entity having been identified during a computer-assisted process comprising supplying a computer modeling application with a set of structure coordinates of a molecule or complex, the molecule or complex comprising at least a portion of at least one druggable region from human PDE4D2; supplying the computer modeling application with a set of ~s structure coordinates of a chemical entity; and determining whether the chemical entity is expected to bind or to interfere with the molecule or complex at a druggable region, wherein binding to or interfering with the molecule or complex is indicative of potential inhibition of PDE4D2 activity.
The presently disclosed subject matter also provides a computer 2o readable storage medium comprising digitally encoded data, wherein the data comprises structural coordinates for a druggable region that is structurally homologous to the structure coordinates as listed in Table 4 or Table 5 for a druggable region of human PDE4D2.
The presently disclosed subject matter also provides a computer 2s readable storage medium comprising digitally encoded structural data, wherein the data comprise a majority of the three-dimensional structure coordinates as listed in Table 4 or Table 5. In one embodiment, the computer readable storage medium further comprises the identity of the atoms for the majority of the three-dimensional structure coordinates as so listed in Table 4 or Table 5. In another embodiment, the data comprise substantially all of the three-dimensional structure coordinates as listed in Table 4 or Table 5.

Accordingly, it is an object of the presently disclosed subject matter to provide three-dimensional structures of an unliganded PDE4D2 catalytic domain and of a PDE4D2 catalytic domain in complex with a ligand. The object is achieved in whole or in part by the presently disclosed subject s matter.
An object of the presently.disclosed subject matter having been stated hereinabove, other objects will be evident~as the description proceeds, when taken in connection with the accompanying Drawings and Examples as described hereinbelow.
1o Brief Descrilation of the Drawings Figures 1A-1C depict the catalytic domain of PDE4D2.
Figure 1A is a ribbon diagram of monomeric PDE4D2. AMP is shown in stick form while two divalent metals are indicated by spheres.
Figure 1B depicts a tetramer of PDE4D2. In each monomer, AMP is 15 depicted as small spheres and metal ions are depicted as large spheres.
Figure 1 C is a comparison of the sequences of the catalytic domain of two PDE4 molecules. The metal binding residues (His164, His200, Asp201, and Asp318) are in bold while the AMP binding residues are underlined.
The bars above the sequences represent helices common to both PDE4B
2o and PDE4D. The most C-terminal bar indicates a helix present only in PDE4B.
Figures 2A and 2B depict AMP binding.
Figure 2A is a stereoview of electron density for AMP, which was calculated from the omitted (Fo - Fc) map and contoured at 3.5 sigmas.
25 Figure 2B depicts AMP interactions with the active site residues. The metal binding residues are shown in purple.
Figure 3 depicts the interactions of the metal ions of PDE4 with AMP.
Dotted lines represent the hydrogen bonds to the metals. The hydrogen bonds between the phosphate of AMP and water molecules W3, W4, and so W5 are not shown. Me2 represents the location of the second metal ion.
Figure 4 illustrates ~a putative mechanism for the hydrolysis of the phosphodiester bond by PDE4.

Brief Description of the Sequences in the Seauence Listing SEQ ID N0:1 is a nucleotide sequence encoding a human PDE4D2 polypeptide (GenBank accession number AF012074).
SEQ fD N0:2 is the amino acid sequence encoded by SEQ ID N0:1.
s SEQ ID N0:3 is a nucleotide sequence encoding a PDE4D2 catalytic domain polypeptide, the polypeptide corresponding to amino acids 79-438 of the human PDE4D2 polypeptide.
SEQ ID N0:4 is the amino acid sequence encoded by SEQ ID N0:3.
Detailed Description ~o Cyclic nucleotide phosphodiesterases (PDEs) regulate the intracellular concentrations of cyclic 3',5'-adenosine and guanosine monophosphate (CAMP and cGMP, respectively) by hydrolyzing them to AMP and GMP. Family-selective inhibitors of PDEs have been studied for treatment of various human diseases. However, the catalytic mechanism of cyclic nucleotide hydrolysis by PDE is not clear. Disclosed herein in alternative embodiments are the resolutions of two crystal structures of a human PDE4D2 catalytic domain at 2.3 A resolution: one unliganded and one in complex with AMP. In the representative structure of PDE4D2-AMP, two divalent metal ions simultaneously interact with the phosphate group of 2o AMP, implying a binuclear catalysis. In addition, the structure revealed a water molecule that binds to the second metal ion and forms hydrogen bonds with GIu230 and a phosphate oxygen of AMP. While the co-inventors do not wish to be bound by any particular theory of operation, a catalytic mechanism in which GIu230, a conserved residue in all PDEs, activates this 2s water molecule to serve as a nucleophile for the hydrolysis of the cAMP
phosphodiester bond is proposed.
Until disclosure of the presently disclosed subject matter presented herein, the ability to obtain crystalline forms of a PDE4D2 catalytic domain, particularly in a complex with a substrate/product, has not been realized.
3o And until the present disclosure, a detailed three-dimensional crystal structure of an unbound PDE4D2 catalytic domain polypeptide and a PDE4D2 catalytic domain polypeptide in complex with a substratelproduct has not been solved.

In addition to providing structural information, crystalline polypeptides provide other advantages. For example, the crystallization process itself further purifies the polypeptide, and satisfies one of the classical criteria for homogeneity. In fact, crystallization frequently provides unparalleled 5 purification quality, removing impurities that are not removed by other purification methods such as HPLC, dialysis, conventional column chromatography, etc. Moreover, crystalline polypeptides are often stable at ambient temperatures and free of protease contamination and degradation associated with solution storage. Crystalline polypeptides can also be useful ~o as pharmaceutical preparations. Finally, crystallization techniques are generally free of problems such as denaturation associated with other stabilization methods(i.e., lyophilization).
Once crystallization has been accomplished, crystallographic data provides useful structural information that can assist the design of 15 compounds that can serve as agonists or antagonists, as described herein below. In addition, the crystal structure provides information that can be used to map the molecular surface of the catalytic domain of PDE4D2. A
small non-peptide molecule designed to mimic portions of this surface could serve as a modulator of PDE4D2 catalytic activity.
2o I. Definitions Before the present proteins, nucleotide sequences, and methods are described, it is understood that the presently disclosed subject matter is not limited to the particular methodology, protocols, cell lines, vectors, and reagents described as these can vary. It is also to be understood that the 25 terminology used herein is for the purpose of describing particular embodiments only, and is not intended to limit the scope of the presently disclosed subject matter.
Unless defined otherwise, all technical and scientific terms used herein are intended to have their ordinary meanings as understood by one of 30 ordinary skill in the art to which presently disclosed subject matter pertains.
Although any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the presently disclosed subject matter, the preferred methods, devices, and materials are now described. All publications mentioned herein are incorporated by reference for the purpose of describing the cell lines, vectors, reagents, and methodologies they disclose.
For convenience, certain terms employed in the specification, s examples, and appended claims are collected here. Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which presently disclosed subject matter belongs.
Following long-standing patent law convention, the articles "a" and

10 "an" are used herein to refer to one or to more than one (i.e., to at least one) of the grammatical object of the article. By way of example, "an element"
means one element or more than one element.
As used herein, the term "agonist" refers to an agent that supplements or potentiates a biological activity of a functional PDE4D2 gene 15 or protein, or of a polypeptide encoded by a gene that is up- or down regulated by a PDE4D2 polypeptide, and/or a polypeptide encoded by a gene that contains a PDE4D2 binding site or response element in its promoter region.
As used herein, the term "antagonist" refers to an agent that 2o decreases or inhibits the biological activity of a functional gene or protein (for example, a functional PDE4D2 gene or protein), or that supplements or potentiates the biological activity of a naturally occurring or engineered non functional gene or protein (for example, a non-functional PDE4D2 gene or protein). Alternatively, an antagonist can decrease or inhibit the biological 2s activity of a functional gene or polypeptide encoded by a gene that is up or down regulated by a PDE4D2 polypeptide. An antagonist can also supplement or potentiate the biological activity of a naturally occurring or engineered non-functional gene or polypeptide encoded by a gene that is up or down regulated by a PDE4D2 polypeptide.
3o As used herein, the terms "a-helix" and "alpha-helix" are used interchangeably and refer to a conformation of a polypeptide chain wherein the polypeptide backbone is wound around the long axis of the molecule in a left-handed or right-handed direction, and the R groups of the amino acids protrude outward from the helical backbone, wherein the repeating unit of the structure is a single turn of the helix, which extends about 0.56 nm along the long axis.
As used herein, the terms "amino acid", "amino acid residue", and s "residue" are used interchangeably and refer to an amino acid formed upon chemical digestion (hydrolysis) of a peptide or polypeptide at its peptide linkages. Amino acids can also be synthesized individually or as components of a peptide. In one embodiment, the amino acid residues described herein are in the "L" isomeric form. However, residues in the "D"
isomeric form can be substituted for any L-amino acid residue, provided that the desired functional property is retained by the polypeptide. In the context of an amino acid, NH2 refers to the free amino group present at the amino terminus of a polypeptide, although some amino acids can have NH2 groups at other positions in the amino acid. COOH refers to the free carboxy group ~5 present at the carboxy terminus of a polypeptide. In keeping with standard polypeptide nomenclature, abbreviations for amino acid residues are presented above. The term "amino acid" is intended to embrace all molecules, whether natural or synthetic, which include both an amino functionality and an acid functionality and capable of being included in a 2o polymer of naturally occurring amino acids. Exemplary amino acids include naturally occurring amino acids; analogs, derivatives and congeners thereof;
amino acid analogs having variant side chains; and all stereoisomers of any of the foregoing.
It is noted that amino acid residue sequences represented herein by 25 formulae have a left-to-right orientation in the conventional direction of amino terminus to carboxy terminus. In addition, the terms "amino acid", "amino acid residue", and "residue" are broadly defined to include the amino acids listed in the above table and modified or unusual amino acids. Furthermore, it is noted that a dash at the beginning or end of an amino acid residue 3o sequence indicates a peptide bond to a further sequence of one or more amino acid residues or a covalent bond to an amino-terminal group such as NH2 or acetyl or to a carboxy-terminal group such as COOH.

As used herein, the terms "~3-sheet" and "beta-sheet" are used interchangeably and refer to the conformation of a polypeptide chain stretched into an extended zigzag conformation. Portions of polypeptide chains that run parallel" all run in the same direction. Polypeptide chains that are "anti-parallel" run in the opposite direction from the parallel chains or from each other.
The term "binding" refers to an association, which may be a stable association, between two molecules, i.e., between a polypeptide of the presently disclosed subject matter and a binding partner, due to, for example, electrostatic, hydrophobic, ionic, and/or hydrogen-bond interactions under physiological conditions.
As used herein, the terms "binding site of the PDE4D2 catalytic domain", "PDE4D2 catalytic site", and "PDE4D2 binding site" are used interchangeably, and refer to a cavity within the PDE4D2 catalytic domain vs where a ligand (i.e. cAMP) binds. This cavity can be empty, or can contain water molecules or other molecules from the solvent, or can contain ligand atoms. The "main" binding pocket includes the region of space not occupied by atoms of PDE4D2 that is approximately encompassed or bounded by PDE4D2 residues Tyr159, His160, His164, His200, Asp201, Met273, 2o Asp318, Leu319, Asn321, Thr333, I1e336, Phe340, GIn369, and Phe372.
The binding pocket also includes small regions near to and contiguous with the "main" binding pocket that not occupied by atoms of PDE4D2.
As used herein the term "biological activity" refers to any biochemical function of a biological molecule. A biological activity includes, but is not 2s limited to an interaction with another biological molecule (for example, a polypeptide, a nucleic acid, or a combination thereof). As such, a biological activity results in a biochemical effect including, but not limited to the hydrolysis of a cyclic nucleoside monophosphate.
A "comparison window," as used herein, refers to a conceptual 3o segment of at least 20 contiguous amino acid positions wherein a protein sequence may be compared to a reference sequence of at least 20 contiguous amino acids and wherein the portion of the protein sequence in the comparison window may comprise additions or deletions (i.e., gaps) of 20 percent or less as compared to the reference sequence (which does not comprise additions or deletions) for optimal alignment of the two sequences.
Optimal alignment of sequences for aligning a comparison window may be conducted by the local homology algorithm of Smith and Waterman (1981) s Adv. Appl. Math. 2: 482, by the homology alignment algorithm of Needleman and Wunsch (1970) J. Mol. Biol. 48: 443, by the search for similarity method of Pearson and Lipman (1988) Proc. Nat!. Acad. Sci. (U.S.A.) 85: 2444, by computerized implementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, available from ~o Accelrys, Inc., San Diego, California, United States of America), or by inspection, and the best alignment (i.e., resulting in the highest percentage of homology over the comparison window) generated by the various methods may be identified.
The term "complex" refers to an association between at least two moieties (i.e. chemical or biochemical) that have an affinity for one another.
Examples of complexes include associations between antigen/antibodies, lectiniavidin, target polynucleotidelprobe oligonucleotide, antibodylanti-antibody, receptor/ligand, enzyme/ligand, polypeptidel polypeptide, polypeptidelpolynucleotide, polypeptidelco-factor, polypeptide/substrate, 2o polypeptideiinhibitor, polypeptide/small molecule, and the like. "Member of a complex" refers to one moiety of the complex, such as an antigen or ligand.
"Protein complex" or "polypeptide complex" refers to a complex comprising at least one polypeptide.
The term "conserved residue" refers to an amino acid that is a 2s member of a group of amino acids having certain common properties. The term "conservative amino acid substitution" refers to the substitution (conceptually or otherwise) of an amino acid from one such group with a different amino acid from the same group. A functional way to define common properties between individual amino acids is to analyze the 3o normalized frequencies of amino acid changes between corresponding proteins of homologous organisms (Schulz, G. E. and R. H. Schirmer., Principles of Protein Structure, Springer-Verlag). According to such analyses, groups of amino acids may be defined where amino acids within a group exchange preferentially with each other, and therefore resemble each other most in their impact on the overall protein structure (Schulz, G. E. and R. H. Schirmer, Principles of Protein Structure, Springer-Verlag). One example of a set of amino acid groups defined in this manner include: (i) a charged group, consisting of Glu and Asp, Lys, Arg and His, (ii) a positively-charged group, consisting of Lys, Arg and His, (iii) a negatively-charged group, consisting of Glu and Asp, (iv) an aromatic group, consisting of Phe, Tyr and Trp, (v) a nitrogen ring group, consisting of His and Trp, (vi) a large aliphatic nonpolar group, consisting of Val, Leu and Ile, (vii) a slightly-polar ~o group, consisting of Met and Cys, (viii) a small-residue group, consisting of Ser, Thr, Asp, Asn, Giy, Ala, Glu, Gln and Pro, (ix) an aliphatic group consisting of Val, Leu, Ile, Met and Cys, and (x) a small hydroxyl group consisting of Ser and Thr.
As used herein, the term "DNA segment" refers to a DNA molecule 15 that has been isolated free of total genomic DNA of a particular species.
In one embodiment, a DNA segment encoding a PDE4D2 polypeptide refers to a nucleic acid comprising SEQ ID NO: 1. 1n another embodiment, a DNA
segment encoding a PDE4D2 polypeptide refers to a nucleic acid comprising SEQ ID NO: 3. DNA segments can comprise a portion of a recombinant 2o vector, including, for example, a plasmid, a cosmid, a phage, a virus, and the like.
As used herein, the term "DNA sequence encoding a PDE4D2 polypeptide" also refers to one or more coding sequences within a particular individual. Moreover, certain differences in nucleotide sequences can exist 2s between individual organisms, which are called alleles. It is possible that such allelic differences might or might not result in differences in amino acid sequence of the encoded polypeptide yet still encode a protein with the same biological activity. As is well known, genes for a particular polypeptide can exist in single or multiple copies within the genome of an individual.
3o Such duplicate genes can be identical or can have certain modifications, including nucleotide substitutions, additions, or deletions, all of which still code for polypeptides having substantially the same activity.

The term "domain", when used in connection with a polypeptide, refers to a specific region within such polypeptide that comprises a particular structure or mediates a particular function. In the typical case, a domain of a polypeptide of the presently disclosed subject matter is a fragment of the polypeptide. In certain instances, a domain is a structurally stable domain, as evidenced, for example, by mass spectroscopy, or by the fact that a modulator may bind to a druggable region of the domain.
The term "druggable region", when used in reference to a polypeptide, nucleic acid, complex and the like, refers to a region of the molecule which is ~o a target or is a likely target for binding a modulator. For a polypeptide, a druggable region generally refers to a region wherein several amino acids of a polypeptide would be capable of interacting with a modulator or other molecule. For a polypeptide or complex thereof, exemplary druggable regions including binding pockets and sites, enzymatic active sites, interfaces between domains of a polypeptide or complex, surface grooves or contours or surfaces of a polypeptide or complex which are capable of participating in interactions with another molecule. In certain instances, the interacting molecule is another polypeptide, which may be naturally occurring. In other instances, the druggable region is on the surface of the 2o molecule.
Druggable regions may be described and characterized in a number of ways. For example, a druggable region may be characterized by some or afl of the amino acids that make up the region; or the backbone atoms thereof, or the side chain atoms thereof (optionally with or without the Coc 25 atoms). Alternatively, in certain instances, the volume of a druggable region corresponds to that of a carbon based molecule of at least about 200 amu and often up to about 800 amu. In other instances, it will be appreciated that the volume of such region may correspond to a molecule of at least about 600 amu and often up to about 1600 amu or more.
30 Alternatively, a druggable region may be characterized by comparison to other regions on the same or other molecules. For example, the term "affinity region" refers to a druggable region on a molecule (such as a polypeptide of the presently disclosed subject matter) that is present in several other molecules, in so much as the structures of the same affinity regions are sufficiently the same so that they are expected to bind the same or related structural analogs. An example of an affinity region is an ATP-binding site of a protein kinase that is found in several protein kinases (whether or not of the same origin). The term "selectivity region" refers to a druggable region of a molecule that may not be found on other molecules, in so much as the structures of different selectivity regions are sufficiently different so that they are not expected to bind the same or related structural analogs. An exemplary selectivity region is a catalytic domain of a protein 1o kinase that exhibits specificity for one substrate. In certain instances, a single modulator may bind to the same affinity region across a number of proteins that have a substantially similar biological function, whereas the same modulator may bind to only one selectivity region of one of those proteins.
~5 Continuing with examples of different druggable regions, the term "undesired region" refers to a druggable region of a molecule that upon interacting with another molecule results in an undesirable affect. For example, a binding site that oxidizes the interacting molecule (such as cytochrome P450 activity) and thereby results in increased toxicity for the 20 oxidized molecule may be deemed a "undesired region". Other examples of potential undesired regions includes regions that upon interaction with a drug decrease the membrane permeability of the drug, increase the excretion of the drug, or increase the blood brain transport of the drug. It may be the case that, in certain circumstances, an undesired region will no longer be 2s deemed an undesired region because the affect of the region will be favorable, i.e., a drug intended to treat a brain condition would benefit from interacting with a region that resulted in increased blood brain transport, whereas the same region could be deemed undesirable for drugs that were not intended to be delivered to the brain.
30 When used in reference to a druggable region, the "selectivity" or "specificity' of a molecule such as a modulator to a druggable region may be used to describe the binding between the molecule and a druggable region.
For example, the selectivity of a modulator with respect to a druggable region may be expressed by comparison to another modulator, using the respective values of Kd (i.e., the dissociation constants for each modulatvr-druggable region complex) or, in cases where a biological effect is observed below the Kd, the ratio of the respective ECSO's (i.e., the concentrations that produce 50°1° of the maximum response for the modulator interacting with each druggable region).
As used herein, the term "expression" generally refers to the cellular processes by which a biologically active polypeptide is produced. As such, the term "expression" generally includes those cellular processes that begin ~o with transcription and end with the production of a functional polypeptide.
As used herein, "expression" is also intended to refer to cellular processes by which a polypeptide is produced that would otherwise be functional except for the presence of mutations in the nucleotide sequence encoding it.
Consistent with this usage, "expression" includes, but is not limited to such 15 processes as transcription, translation, post-translational modification, and transport of a polypeptide.
A "fusion protein" or "fusion polypeptide" refers to a chimeric protein as that term is known in the art and may be constructed using methods known in the art. In many examples of fusion proteins, there are two 2o different polypeptide sequences, and in certain cases, there may be more.
The sequences may be linked in frame. A fusion protein may include a domain that is found (albeit in a different protein) in an organism that also expresses the first protein, or it may be an "interspecies", "intergenic", etc.
fusion expressed by different kinds of organisms. In various embodiments, 2s the fusion polypeptide may comprise one or more amino acid sequences linked. to a first polypeptide. In the case where more than one amino acid sequence is fused to a first polypeptide, the fusion sequences may be multiple copies of the same sequence, or alternatively, may be different amino acid sequences. The fusion polypeptides may be fused to the N-ao terminus, the C-terminus, or the N- and C-terminus of the first polypeptide.
Exemplary fusion proteins include polypeptides comprising a glutathione S-transferase tag.(GST-tag), histidine tag (His-tag), an immunoglobulin domain or an immunoglobulin binding domain.

As used herein, the term "gene" is used for simplicity to refer to nucleotide sequence that encodes a protein, polypeptide, or peptide. As such, the term "gene" refers to a nucleic acid comprising an open reading frame encoding a polypeptide having exon sequences and optionally intron s sequences. The term "intron" refers to a DNA sequence present in a given gene that is not translated into protein and is generally found between exons. As will be understood by those of skill in the art, this functional term includes both genomic sequences and cDNA sequences. Representative embodiments of such sequences are disclosed herein.
~o The term "having substantially similar biological activity", when used in reference to two polypeptides, refers to a biological activity of a first polypeptide which is substantially similar to at feast one of the biological activities of a second polypeptide. A substantially similar biological activity means that the polypeptides carry out a similar function, i.e., a similar enzymatic reaction or a similar physiological process, etc. For example, two homologous proteins may have a substantially similar biological activity if they are involved in a similar enzymatic reaction, i.e., they are both kinases which catalyze phosphorylation of a substrate polypeptide, however, they may phosphorylate different regions on the same protein substrate or 2o different substrate proteins altogether. Alternatively, two homologous proteins may also have a substantially similar biological activity if they are both involved in a similar physiological process, i.e., transcription. For example, two proteins may be transcription factors, however, they may bind to different DNA sequences or bind to different polypeptide interactors.
2s Substantially similar biological activities may also be associated with proteins carrying out a similar structural role, for example, two membrane proteins.
As used herein, the term "interact" refers to detectable interactions between molecules, such as can be detected using, for example, a yeast two-hybrid assay. The term "interact" is also meant to include "binding"
3o interactions between molecules. Interactions include, but are not limited to protein-protein, protein-nucleic acid, and protein-small molecule interactions.
These interactions can be in the form of covalent or non-covalent interactions including, but not limited to ionic, hydrogen bonding, and van der Waals interactions.
As used herein, the term "isolated" refers to a nucleic acid substantially free of other nucleic acids, proteins, lipids, carbohydrates, or other materials with which it can be associated, such association being either in cellular material or in a synthesis medium. The term can also be applied to polypeptides, in which case the polypeptide is substantially free of nucleic acids, carbohydrates, lipids, and other undesired polypeptides. The term "isolated polypeptide" refers to a polypeptide, in certain embodiments 1o prepared from recombinant DNA or RNA, or of synthetic origin, or some combination thereof, which (1 ) is not associated with proteins that it is normally found with in nature, (2) is isolated from the cell in which it normally occurs, (3) is isolated free of other proteins from the same cellular source, (4) is expressed by a cell from a different species, or (5) does not occur in nature.
The term "isolated nucleic acid" refers to a polynucleotide of genomic, cDNA, or synthetic origin or some combination there of, which (1 ) is not associated with the cell in which the "isolated nucleic acid" is found in nature, or (2) is operably linked to a polynucleotide to which it is not linked in nature.
2o The terms "label" or "labeled" refer to incorporation or attachment, optionally covalently or non-covalently, of a detectable marker into a molecule, such as a polypeptide. Various methods of labeling polypeptides are known in the art and may be used. Examples of labels for polypeptides include, but are not limited to, the following: radioisotopes, fluorescent labels, 25 heavy atoms, enzymatic labels or reporter genes, chemiluminescent groups, biotinyl groups, predetermined polypeptide epitopes recognized by a secondary reporter (i.e., leucine zipper pair sequences, binding sites for secondary antibodies, metal binding domains, epitope tags). Examples and use of such labels are described in more detail below. In some 3o embodiments, labels are attached by spacer arms of various lengths to reduce potential steric hindrance.
' 34 The term "mammal" is known in the art, and exemplary mammals include humans, primates, bovines, porcines, canines, felines, and rodents (i.e., mice and rats).
The term "modulation", when used in reference to a functional s property or biological activity or process (i.e., enzyme activity or receptor binding), refers to the capacity to either up regulate (i.e., activate or stimulate), down regulate (i.e., inhibit or suppress) or otherwise change a quality of such property, activity, or process. In certain instances, such regulation may be contingent on the occurrence of a specific event, such as activation of a signal transduction pathway, andlor may be manifest only in particular cell types.
The term "modulator" refers to a polypeptide, nucleic acid, macromolecule, complex, molecule, small molecule, compound, species or the like (naturally-occurring or non-naturally-occurring), or an extract made 15 from biological materials such as bacteria, plants, fungi, or animal- cells or tissues, that may be capable of causing modulation. Modulators may be evaluated for potential activity as inhibitors or activators (directly or indirectly) of a functional property, biological activity or process, or combination of them, (i.e., agonist, partial antagonist, partial agonist, inverse agonist, 2o antagonist, anti-microbial agents, inhibitors of microbial infection or proliferation, and the like) by inclusion in assays. In such assays, many modulators may be screened at one time. The activity of a modulator may be known, unknown or partially known.
As used herein, the term "molecular replacement" refers to a method 2s that involves generating a preliminary model of the wild-type PDE4D2 catalytic domain or a PDE4D2 mutant crystal the structure for which coordinates are unknown, by orienting and positioning a molecule the structure for which coordinates are known within the unit cell of the unknown crystal so as best to account for the observed diffraction pattern of the so unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure the coordinates for which are unknown. This, in turn, can be subjected to any of the several forms of refinement known in the art to provide a final, accurate structure of the unknown crystal. (Lattman, Meth Enzymol, 115:55-77, 1985; Rossmann, ed., The Molecular Replacement Method, Gordon & Breach, New York, 1972.) Using the structure coordinates of the catalytic domain of PDE4D2 provided by presently disclosed subject matter, molecular replacement can be used to determine the structure coordinates of a crystal of a mutant or of a homologue of the PDE4D2 catalytic domain, or of a different crystal form of the PDE4D2 catalytic domain.
The term "moti~P' refers to an amino acid sequence that is commonly ~o found in a protein of a particular structure or function. Typically, a consensus sequence is defined to represent a particular motif. The consensus sequence need not be strictly defined and may contain positions of variability, degeneracy, variability of length, etc. The consensus sequence may be used to search a database to identify other proteins that may have a ~s similar structure or function due to the presence of the motif in its amino acid sequence. For example, on-line databases may be searched with a consensus sequence in order to identify other proteins containing a particular motif. Various search algorithms and/or programs may be used, including FASTA, BLAST or ENTREZ. FASTA and BLAST are available as 2o a part of the GCG sequence analysis package (Accelrys, Inc., San Diego, California, United States of America). ENTREZ is available through the National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland, United States of America.
As used herein, the term "mutation" carries its traditional connotation 25 and refers to a change, inherited, naturally occurring, or introduced, in a nucleic acid or polypeptide sequence, and is used in its sense as generally known to those of skill in the art.
The term "naturally occurring", as applied to an object, refers to the fact that an object may be found in nature. For example, a polypeptide or 3o polynucleotide sequence that is present in an organism (including bacteria) that may be isolated from a source in nature and which has not been intentionally modified by man in the laboratory is naturally occurring.

The term "nucleic acid" refers to a polymeric form of nucleotides, either ribonucleotides or deoxynucleotides or a modified form of either type of nucleotide. The terms should also be understood to include, as equivalents, analogs of either RNA or DNA made from nucleotide analogs, s and, as applicable to the embodiment being described, single-stranded (such as sense or antisense) and double-stranded polynucleotides.
The term "nucleic acid of the presently disclosed subject matter"
refers to a nucleic acid encoding a polypeptide of the presently disclosed subject matter, i.e., a nucleic acid comprising a sequence consisting of, or ~o consisting essentially of, the polynucleotide sequence set forth in SEQ ID
NO: 1 or SEQ ID NO: 3. A nucleic acid of the presently disclosed subject matter may comprise all, or a portion of: the nucleotide sequence of SEQ ID
NO: 1 or SEQ ID NO: 3; a nucleotide sequence at least 60%, 70%, 80%, 90°l°, 95%, 96%, 97%, 98% or 99% identical to SEQ ID NO: 1 or SEQ ID
NO: 3; a nucleotide sequence that hybridizes under stringent conditions to SEQ ID NO: 1 or SEQ ID NO: 3; nucleotide sequences encoding polypeptides that are functionally equivalent to polypeptides of the presently disclosed subject matter; nucleotide sequences encoding polypeptides at least about 60%, 70%, 80%, 85%, 90%, 95%, 98%, 99% homologous or 2o identical with an amino acid sequence of SEQ ID NO: 2 or SECT ID NO: 4;
nucleotide sequences encoding polypeptides having an activity of a polypeptide of the presently disclosed subject matter and having at least about 60%, 70%, 80%, 85%, 90%, 95%, 98°t°, 99°!°
or more homology or identity with SEC, ID NO: 2 or SEQ ID NO: 4; nucleotide sequences that 2s differ by 1 to about 2, 3, 5, 7, 10, 15, 20, 30, 50, 75 or more nucleotide substitutions, additians or deletions, such as allelic variants, of SEQ ID NO:
1 and SEQ ID NO: 3; nucleic acids derived from and evolutionarily related to SEQ ID NO: 1 or SEQ ID NO: 3; and complements of, and nucleotide sequences resulting from the degeneracy of the genetic code, for all of the 3o foregoing and other nucleic acids of the presently disclosed subject matter.
Nucleic acids of the presently disclosed subject matter also include homologs, i.e., orthologs and paralogs, of SEQ ID NO: 1 or SEQ ID NO: 3 and also variants of SEQ ID NO: 1 or SEQ ID NO: 3 which have been codon optimized for expression in a particular organism (i.e., host cell).
The term "operably linked", when describing the relationship between two nucleic acid regions, refers to a juxtaposition wherein the regions are in s a relationship permitting them to function in their intended manner. For example, a control sequence "operably linked" to a coding sequence is ligated in such a way that expression of the coding sequence is achieved under conditions compatible with the control sequences, such as when the appropriate molecules (i.e., inducers and polymerases) are bound to the 1o control or regulatory sequence(s).
As used herein, "orthorhombic unit cell" refers to a unit cell wherein a ~ b ~ c; and a = ~ = y = 90°. The vectors a, b, and c describe the unit cell edges and the angles a, ~3, and y describe the unit cell angles.
As used herein, the term "PDE4D2" refers to any polypeptide with an ~s amino acid sequence that can be aligned with at least one of human, mouse, or rat PDE4D2, such that at least 50% of the amino acids are identical to the corresponding amino acid in the human, mouse, or rat PDE4D2. The term "PDE4D2" also encompasses nucleic acids for which the corresponding translated protein sequence can be considered to be a PDE4D2. The term 20 "PDE4D2" includes vertebrate homologs of PDE4D2 family members including, but not limited to mammalian and avian homologs.
Representative mammalian homologs of PDE4D2 family members include, but are not limited to murine and human homologs.
As used herein, the terms "PDE4D2 gene" and "recombinant PDE4D2 2s gene" are used interchangeably and refer to a nucleic acid molecule comprising an open reading frame encoding a PDE4D2 polypeptide, including both exon and (optionally) intron sequences.
As used herein, the terms "PDE4D2 gene product", "PDE4D2 protein", "PDE4D2 polypeptide", and "PDE4D2 peptideH are used 3o interchangeably and refer to peptides having amino acid sequences which are substantially identical to native PDE4D2 amino acid sequences from the organism of interest and which are biologically active in that they comprise all or a part of the amino acid sequence of a PDE4D2 polypeptide, or cross-react with antibodies raised against a PDE4D2 polypeptide, or retain all or some of the biological activity (i.e., catalytic ability andlor dimerization ability) of the native amino acid sequence or protein. Such biological activity can include immunogenicity.
s As used herein, the terms "PDE4D2 gene product", "PDE4D2 protein", "PDE4D~ polypeptide", and "PDE4D2 peptide" are used interchangeably and refer to a subtype of the PDE4D2 family. In one embodiment, a PDE4D2 gene product is PDE4D2. In another embodiment, a PDE4D2 gene product comprises the amino acid sequence of SEQ ID NO:
~0 2.
As used herein, the terms "PDE4D2 gene product", "PDE4D2 protein", "PDE4D2 polypeptide", and "PDE4D~ peptide" also include analogs of a PDE4D2 polypeptide. By "analog" is intended that a DNA or peptide sequence can contain alterations relative to the sequences disclosed herein, 15 yet retain all or some of the biological activity of those sequences.
Analogs can be derived from genomic nucleotide sequences as are disclosed herein or those from other organisms, or can be created synthetically. Those skilled in the art will appreciate that other analogs, as yet undisclosed or undiscovered, can be used to design and/or construct PDE4D2 analogs.
2o There is no need for a "PDE4D2 gene product", "PDE4D2 protein", "PDE4D2 polypeptide", or "PDE4D2 peptide" to comprise all or substantially all of the amino acid sequence of a PDE4D2 polypeptide gene product. Shorter or longer sequences are anticipated to be of use in the presently disclosed subject matter; shorter sequences are herein referred to as "segments".
2s Thus, the terms "PDE4D2 gene product", "PDE4D2 protein", "PDE4D2 polypeptide", and "PDE4D2 peptide" also include fusion or recombinant PDE4D2 polypeptides and proteins comprising sequences of the presently disclosed subject matter. Methods of preparing such proteins are disclosed herein and are known in the art.
so The term "phenotype" refers to the entire physical, biochemical; and physiological makeup of a cell, i.e., having any one trait or any group of traits.

As used herein, the term "polypeptide" refers to' any polymer comprising any of the 20 protein amino acids, regardless of its size.
Although "protein°' is often used in reference to relatively large polypeptides and "peptide°' is often used in reference to small polypeptides, usage of s these terms in the art overlaps and varies. The term "polypeptide" as used herein refers to peptides, polypeptides, and proteins, unless otherwise noted. As used herein, the terms "protein", "polypeptide" and °'peptide" are used interchangeably herein when referring to a gene product. The term "polypeptide", and the terms "protein" and "peptide" which are used ~o interchangeably herein, refers to a polymer of amino acids. Exemplary polypeptides include gene products, naturally occurring proteins, homologs, orthologs, paralogs, fragments, and other equivalents, variants and analogs of the foregoing.
The terms "polypeptide fragment" or "fragment", when used in ~s reference to a reference poiypeptide, refers to a polypeptide in which amino acid residues are deleted as compared to the reference polypeptide itself, but where the remaining amino acid sequence is usually identical to the corresponding positions in the reference poiypeptide. Such deletions may occur at the amino-terminus or carboxy-terminus of the reference 2o polypeptide, or alternatively both. Fragments typically are at least 5, 6, 8 or amino acids long, at least 14 amino acids long, at least 20, 30, 40 or 50 amino acids long, at least 75 amino acids long, or at least 100, 150, 200, 300, 500 or more amino acids long. A fragment can retain one or more of the biological activities of the reference polypeptide. In certain 2s embodiments, a fragment may comprise a druggable region, and optionally additional amino acids on one or both sides of the druggable region, which additional amino acids may number from 5, 10, 15, 20, 30, 40, 50, or up to 100 or more residues. Further, fragments can include a sub-fragment of a specific region, which sub-fragment retains a function of the region from so which it is derived. In another embodiment, a fragment may have immunogenic properties.
The term "polypeptide of the presently disclosed subject matter refers to a polypeptide comprising the amino acid sequence set forth in SEQ ID

NO: 2 or SEQ ID NO: 4, or an equivalent or fragment thereof, i.e., a polypeptide comprising a sequence consisting of, or consisting essentially of, the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4.
Polypeptides of the presently disclosed subject matter include polypeptides 5 comprising all or a portion of the amino acid sequence set forth in SEQ ID
NO: 2 or SEQ 1D NO: 4; the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4 with 1 to about 2, 3, 5, 7, 10, 15, 20, 30, 50, 75 or more conservative amino acid substitutions; an amino acid sequence that is at least 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, or 99% identical to SEQ
~o ID NO: 2 or SEQ ID NO: 4; and functional fragments thereof. Polypeptides of the presently disclosed subject matter also include homologs, i.e., orthologs and paralogs, of SEQ ID NO: 2 or SEQ ID NO: 4.
As used herein, the term "primer" refers to a nucleic acid comprising in one embodiment two or more deoxyribonucleotides or ribonucleotides, in ~s another embodiment more than three, in another embodiment more than eight, and in yet another embodiment at least about 20 nucleotides of an exonic or intronic region. In one embodiment, an oligonucfeotide is between ten and thirty bases in length.
The term "purified" refers to an object species that is the predominant 2o species present (i.e., on a molar basis it is more abundant than any other individual species in the composition). A "purifiied fraction" is a composition wherein the object species comprises at least about 50 percent (on a molar basis) of all species present. In making the determination of the purity of a species in solution or dispersion, the solvent or matrix in which the species is 2s dissolved or dispersed is usually not included in such determination;
instead, only the species (including the one of interest) dissolved or dispersed are taken into account. Generally, a purified composition will have one species that comprises more than about 80 percent of ail species present in the composition, more than about 85%, 90%, 95%, 99% or more of all species 3o present. The object species may be purified to essential homogeneity (contaminant species cannot be detected in the composition by conventional detection methods) wherein the composition consists essentially of a single species. A skilled artisan may purify a polypeptide of the presently disclosed subject matter using standard techniques for protein purification in light of the teachings herein. Purity of a polypeptide may be determined by a number of methods known to those of skill in the art, including for example, amino-terminal amino acid sequence analysis, gel electrophoresis, mass-5 spectrometry analysis and the methods described in the Exemplification section herein.
The terms "recombinant protein" or "recombinant polypeptide" refer to a palypeptide that is produced by recombinant DNA techniques. An example of such techniques includes the case when DNA encoding the expressed protein is inserted into a suitable expression vector that is in turn used to transform a host cell to produce the protein or polypeptide encoded by the DNA.
A "reference sequence" is a defined sequence used as a basis for a sequence comparison; a reference sequence may be a subset of a larger vs sequence, for example, as a segment of a full-length protein given in a sequence listing such as SEQ ID NO: 2 or SEQ ID NO: 4, or may comprise a complete protein sequence. Generally, a reference sequence is at least 200, 300 or 400 nucleotides in length, frequently at least 600 nucleotides in length, and often at least 800 nucleotides in length (or the protein equivalent 2o if it is shorter or longer in length). Because two proteins may each (1 ) comprise a sequence (i.e., a portion of the complete protein sequence) that is similar between the two proteins, and (2) may further comprise a sequence that is divergent between the two proteins, sequence comparisons between two {or more) proteins are typically performed by comparing 25 sequences of the two proteins over a "comparison window" to identify and compare local regions of sequence similarity.
The term "regulatory sequence" is a generic term used throughout the specification to refer to polynucleotide sequences, such as initiation signals, enhancers, regulators and promoters, that are necessary or desirable to 3o affect the expression of coding and non-coding sequences to which they are operably linked. Exemplary regulatory sequences are described in Goeddel;
Gene Expression Technology: Methods in Enzymology, Academic Press, San Diego, CA (1990), and include, for example, the early and late promoters of SV40, adenovirus or cytomegalovirus immediate early promoter, the lac system, the trp system, the TAC or TRC system, T7 promoter whose expression is directed by T7 RfVA polymerase, the major operator and promoter regions of phage lambda, the control regions for fd s coat protein, the promoter for 3-phosphoglycerate kinase or other glycolytic enzymes, the promoters of acid phosphatase, i.e., PhoS, the promoters of the yeast a-mating factors, the polyhedron promoter of the baculovirus system and other sequences known to control the expression of genes of prokaryotic or eukaryotic cells or their viruses, and various combinations thereof. The nature and use of such control sequences may differ depending upon the host organism. In prokaryotes, such regulatory sequences generally include promoter, ribosomal binding site, and transcription termination sequences. The term "regulatory sequence" is intended to include, at a minimum, components whose presence may influence expression, and may also include additional components whose presence is advantageous, for example, leader sequences and fusion partner sequences. In certain embodiments, transcription of a polynucleotide sequence is under the control of a promoter sequence (or other regulatory sequence) that controls the expression of the polynucleotide 2o in a cell-type in which expression is intended. It will also be understood that the polynucleotide can be under the control of regulatory sequences that are the same or different from those sequences which control expression of the naturally occurring form of the polynucleotide.
The term "reporter gene" refers to a nucleic acid comprising a 2s nucleotide sequence encoding a protein that is readily detectable either by its presence or activity, including, but not limited to, luciferase, fluorescent protein (i.e., green fluorescent protein), chlorar~iphenicol acetyl transferase, ~-galactosidase, secreted placental alkaline phosphatase, a-factamase, human growth hormone, and other secreted enzyme reporters. Generally, a 3o reporter gene encodes a polypeptide not otherwise produced by the host cell, which is detectable by analysis of the cell(s), i.e., by the direct fluorometric, radioisotopic or spectrophotometric analysis of the cells) and preferably without the need to kill the cells for signal analysis. In certain instances, a reporter gene encodes an enzyme, which produces a change in fluorometric properties of the host cell, which is detectable by qualitative, quantitative, or semiquantitative function or transcriptional activation.
Exemplary enzymes include esterases, ~-lactamase, ' phosphatases, s peroxidases, proteases (tissue plasminogen activator or urokinase) and other enzymes whose function may be detected by appropriate chromogenic or fluorogenic substrates known to those skilled in the art or developed in the future.
The term "sequence homology" refers to the proportion of base 1o matches between two nucleic acid sequences or the proportion of amino acid matches between two amino acid sequences. When sequence homology is expressed as a percentage, i.e., 50%, the percentage denotes the proportion of matches over the length of sequence from a desired sequence (i.e., SEQ. ID NO: 1) that is compared to some other sequence.
~s Gaps (in either of the two sequences) are permitted to maximize matching;
gap lengths of 15 bases or less are usually used, 6 bases or less are used more frequently, with 2 bases or less used even more frequently. The term "sequence identity" means that sequences are identical (i.e., on a nucleotide-by-nucleotide basis for nucleic acids or amino acid-by-amino acid 2o basis for polypeptides) over a window of comparison. The term "percentage of sequence identity" is calculated by comparing two optimally aligned sequences over the comparison window, determining the number of positions at which the identical amino acids occurs in both sequences to yield the number of matched positions, dividing the number of matched 2s positions by the total number of positions in the comparison window, and multiplying the result by 100 to yield the percentage of sequence identity.
Methods to calculate sequence identity are known to those of skill in the art and described in further detail herein.
As used herein, the term "sequencing" refers to determining the 30 ordered linear sequence of nucleotides or amino acids of a DNA, RNA, or protein target sample, using conventional manual or automated laboratory techniques.

The term "small molecule" refers to a compound, which has a molecular weight of less than about 5 kilodalton (kD), less than about 2.5 kD, less than about 1.5 kD, or less than about 0.9 kD. Small molecules may be, for example, nucleic acids, peptides, polypeptides, peptide nucleic acids, 5 peptidomimetics, carbohydrates, lipids, or other organic (carbon containing) or inorganic molecules. Many pharmaceutical companies have extensive libraries of chemical and/or biological mixtures, often fungal, bacterial, or algal extracts, which can be screened with any of the assays of the presently disclosed subject matter. The term "small organic molecule" refers to a small molecule that is often identified as being an organic or medicinal compound, and does not include molecules that are exclusively nucleic acids, peptides, or polypeptides.
The term "soluble" as used herein with reference to a polypeptide of the presently disclosed subject matter or other protein, means that upon ~5 expression in cell culture, at least some portion of the polypeptide or protein expressed remains in the cytoplasmic fraction of the cell and does not fractionate with the cellular debris upon lysis and centrifugation of the lysate.
Solubility of a polypeptide may be increased by a variety of art recognized methods, including fusion to a heterologous amino acid sequence, deletion 20 of amino acid residues, amino acid substitution (i.e., enriching the sequence with amino acid residues having hydrophilic side chains), and chemical modification (i.e., addition of hydrophilic groups). The solubility of polypeptides may be measured using a variety of art recognized techniques, including, dynamic light scattering to determine aggregation state, UV
25 absorption, centrifugation to separate aggregated from non-aggregated material, and SDS gel electrophoresis (i.e., the amount of protein in the soluble fraction is compared to the amount of protein in the soluble and insoluble fractions combined). When expressed in a host cell, the polypeptides of the presently disclosed subject matter may be at least about 30 1 %, 2%, 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or more soluble, i.e., at least about 1%, 2%, 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or more of the total amount of protein expressed in the cell is found in the cytaplasmic fraction. In certain embodiments, a one liter culture of cells expressing a polypeptide of the presently disclosed subject matter will produce at least about 0.1, 0.2, 0.5, 1, 2, 5, 10, 20, 30, 40, 50 milligrams or more of soluble protein. In an exemplary embodiment, a polypeptide of the presently disclosed subject matter is at least about 10%
s soluble and will produce at least about 1 milligram of protein from a one liter cell culture.
As used herein, the term "space group" refers to the arrangement of symmetry elements of a crystal.
The term "specifically hybridizes" refers to detectable and specific ~o nucleic acid binding. Polynucleotides, oligonucleotides, and nucleic acids of the presently disclosed subject matter selectively hybridize to nucleic acid strands under hybridization and wash conditions that minimize appreciable amounts of detectable binding to nonspecific nucleic acids. Stringent conditions may be used to achieve selective hybridization conditions as 15 known in the art and discussed herein. Generally, the nucleic acid sequence homology between the polynucleotides, oligonucleotides, and nucleic acids of the presently disclosed subject matter and a nucleic acid sequence of interest will be at least 30%, 40%, 50%, 60%, 70%, 80%, 85%, 90%, 95%, 98%, 99%, or more. In certain instances, hybridization and washing 2o conditions are performed under stringent conditions according to conventional hybridization procedures and as described further herein.
As used herein, the terms "structure coordinates", "structural coordinates", and "atomic coordinates" are used interchangeably and refer to coordinates derived from mathematical equations related to the patterns 2s obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of a molecule in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal.
The electron density maps are used to establish the positions of the individual atoms within the unit cell of the crystal.
so Those of skill in the art understand that a set of coordinates determined by X-ray crystallography is not without standard error. In general, the error in the coordinates tends to be reduced as the resolution is increased, since more experimental diffraction data is available for the model fitting and refinement. Thus, for example, more diffraction data can be collected from a crystal that diffracts to a resolution of 2.8-3.2 A than from a crystal that diffracts to a lower resolution, such as 3.5 ~,. Consequently, the refined structural coordinates will usually be more accurate when fitted and s refined using data from a crystal that diffracts to higher resolution. The design of ligands for a PDE4D2 or any other phosphodiesterase depends on the accuracy of the structural coordinates. If the coordinates are not sufficiently accurate, then the design process will be ineffective. In most cases, it is very difficult or impossible to collect sufficient diffraction data to define atomic coordinates precisely when the crystals diffract to a resolution of poorer than 3.5 A. Thus, in most cases, it is difficult to use X-ray structures in structure-based ligand design when the X-ray structures are based on crystals that diffract to a resolution of poorer than 3.5 A. However, common experience has shown that crystals diffracting to 2.8-3.5 A or better ~s can yield X-ray structures with sufficient accuracy to greatly facilitate structure-based drug design. Further improvement in the resolution can further facilitate structure-based design, but the coordinates obtained at 2.8-3.5 A resolution are generally considered adequate for most purposes.
Also, those of skill in the art will understand that PDE4D2 proteins can 2o adopt different conformations when different ligands are bound. PDE4D2 proteins can adopt different conformations when agonists and antagonists are bound. Subtle variations in the conformation can also occur when different agonists are bound, and when different antagonists are bound.
These variations can be difficult or impossible to predict from a single X-ray 25 structure. Generally, structure-based design of PDE4D2 ligands depends to some degree on an understanding of the differences in conformation that occur when agonists and antagonists are bound. Thus, structure-based ligand design is most facilitated by the availability of X-ray structures of complexes with potent agonists as well as potent antagonists.
so The terms "stringent conditions" or "stringent hybridization conditions"
refer to conditions that promote specific hybridization between two complementary polynucleotide strands so as to form a duplex. Stringent conditions may be selected to be about 5°C lower than the thermal melting point (Tm) for a given polynucleotide duplex at a defined ionic strength and pH. The length of the complementary polynucleotide strands and their GC
content will determine the Tm of the duplex, and thus the hybridization conditions necessary for obtaining a desired specificity of hybridization. The Tm is the temperature (under defined ionic strength and pH) at which 50% of a polynucleotide sequence hybridizes to a perfectly matched complementary strand. In certain cases it may be desirable to increase the stringency of the hybridization conditions to be about equal to the Tm for a particular duplex.
A variety of techniques for estimating the Tm are available. Typically, ~o G-C base pairs in a duplex are estimated to contribute about 3°C to the Tm, while A-T base pairs are estimated to contribute about 2°C, up to a theoretical maximum of about 80-100°C. However, more sophisticated models of Tm are available in which G-C stacking interactions, solvent effects, the desired assay temperature and the like are taken into account.
~5 For example, probes can be designed to have a dissociation temperature (Td) of approximately 60°C, using the formula: Td = (((((3 x #GC) + (2 x #AT)) x 37) - 562)/#bp) - 5; where #GC, #AT, and #bp are the number of guanine-cytosine base pairs, the number of adenine-thymine base pairs, and the number of total base pairs, respectively, involved in the formation of the 2o duplex.
Hybridization may be carried out in 5x SSC, 4x SSC, 3x SSC, 2x SSC, 1x SSC or 0.2x SSC for at least about 1 hour, 2 hours, 5 hours, 12 hours, or 24 hours. The temperature of the hybridization may be increased to adjust the stringency of the reaction, for example, from about 25°C
(room 25 temperature), to about 45°C, 50°C, 55°C, 60°C, or 65°C. The hybridization reaction may also include another agent affecting the stringency, for example, hybridization conducted in the presence of 50% formamide increases the stringency of hybridization at a defined temperature.
The hybridization reaction may be followed by a single wash step, or so two or more wash steps, which may be at the same or a different salinity and temperature. For example, the temperature of the wash may be increased to adjust the stringency from about 25°C (room temperature), to about 45°C, 50°C, 55°C, 60°C, 65°C, or higher. The wash step may be conducted in the presence of a detergent, i.e., 0.1 or 0.2% SDS. For example, hybridization may be followed by two wash steps at 65°C each for about 20 minutes in 2x SSC, 0.1 % SDS, and optionally two additional wash steps at 65°C
each for about 20 minutes in 0.2x SSC, 0.1 % SDS.
s Exemplary stringent hybridization conditions include overnight hybridization at 65°C in a solution comprising, or consisting of, 50%
formamide, 10x Denhardt's Solution (0.2% Ficoll, 0.2% Polyvinylpyrrolidone, 0.2% bovine serum albumin) and 200 pg/ml of denatured carrier DNA, i.e., sheared salmon sperm DNA, followed by two wash steps at 65°C each for about 20 minutes in 2x SSC, 0.1 % SDS, and two wash steps at 65°C each for about 20 minutes in 0.2x SSC, 0.1 % SDS
Hybridization may consist of hybridizing two nucleic acids in solution, or a nucleic acid in solution to a nucleic acid attached to a solid support, i.e., a filter. When one nucleic acid is on a solid support, a prehybridization step ~s may be conducted prior to hybridization. Prehybridization may be carried out for at least about 1 hour, 3 hours or 10 hours in the same solution and at the same temperature as the hybridization solution (without the complementary polynucleotide strand).
Appropriate stringency conditions are known to those skilled in the art 20 or may be determined experimentally by the skilled artisan. See, for example, Ausubel et. al., Current Protocols in Molecular Biolopv, John Wiley & Sons, N.Y. (1989), 6.3.1-12.3.6; Sambrook ef al., 1989, Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Press, N.Y; S. Agrawal (ed.) Methods in Molecular Biology, volume 20; Tijssen (1993) Laboratory 25 Technigues in Biochemistry and Molecular Biology-Hybridization With Nucleic Acid Probes, i.e., part I chapter 2 "Overview of principles of hybridization and the strategy of nucleic acid probe assays", Elsevier, New York; and Tibanyenda, N. et al., Eur J. Biochem. 139:19 (1984) and Ebel, S.
et al., 8iochem. 31:12083 (1992).
3o The term "structural motif", when used in reference to a polypeptide, refers to a polypeptide that, although it may have different amino acid sequences, may result in a similar structure, wherein by structure is meant that the motif forms generally the same tertiary structure, or that certain amino acid residues within the motif, or alternatively their backbone or side chains (which may or may not include the Ca atoms of the side chains) are positioned in a like relationship with respect to one another in the motif.
As applied to proteins, the term "substantial identity" means that two s protein sequences, when optimally aligned, such as by the programs GAP or BESTFIT using default gap weights, typically share at least about 70 percent sequence identity; alternatively at least about 80, 85, 90, 95 percent sequence identity or more. In certain instances, residue positions that are not identical differ by conservative amino acid substitutions, which are ~o described above.
As used herein, the term "substantially pure" refers to a polynucleotide or polypeptide that is substantially free of the sequences and molecules with which it is associated in its natural state, as well as from those molecules used in the isolation procedure. The term "substantially 15 free" refers to that the sample is in one embodiment at least 50%, in another embodiment at least 70%, in another embodiment at least 80%, and in still another embodiment at least 90% free of the sequences and molecules with which is it associated in nature.
As used herein, the term "target cell" refers to a cell, into which it is 2o desired to insert a nucleic acid sequence or polypeptide, or to otherwise effect a modification from conditions known to be present in the unmodified cell. A nucleic acid sequence introduced into a target cell can be of variable length. Additionally, a nucleic acid sequence can enter a target cell as a component of a plasmid or other vector or as a naked sequence.
2s The term "test compound" refers to a molecule to be tested by one or more screening methods) as a putative modulator of a polypeptide of the presently disclosed subject matter or other biological entity or process. A
test compound is usually not known to bind to a target of interest. The term "control test compound" refers to a compound known to bind to the target so (i.e., a known agonist, antagonist, partial agonist or inverse agonist).
The term "test compound" does not include a chemical added as a control condition that alters the function of the target to determine signal specificity in an assay. Such control chemicals or conditions include chemicals that 1 ) nonspecifically or substantially disrupt protein structure (i.e., denaturing agents (i.e., urea or guanidinium), chaotropic agents, sulfhydryl reagents (i.e., dithiothreitol and ~-mercaptoethanol), and proteases), 2) generally inhibit cell metabolism (i.e., mitochondria) uncouplers) and 3) non-specifically s disrupt electrostatic or hydrophobic interactions of a protein (i.e., high salt concentrations, or detergents at concentrations sufficient to non-specifically disrupt hydrophobic interactions). Further, the term "test compound" also does not include compounds known to be unsuitable for a therapeutic use for a particular indication due to toxicity of the subject. In certain embodiments, various predetermined concentratians of test compounds are used for screening such as 0.01 ~M, 0.1 p.M, 1.0 ~M, and 10.0 p.M.
Examples of test compounds include, but are not limited to, peptides, nucleic acids, carbohydrates, and small molecules. The term "novel test compound"
refers to a test compound that is not in existence as of the filing date of this ~s application. In certain assays using novel test compounds, the novel test compounds comprise at least about 50%, 75%, 85%, 90%, 95% or more of the test compounds used in the assay or in any particular trial of the assay.
The term "therapeutically effective amount" refers to that amount of a modulator, drug, or other molecule that is sufficient to effect treatment when 2o administered to a subject in need of such treatment. The therapeutically effective amount will vary depending upon the subject and disease condition being treated, the weight and age of the subject, the severity of the disease condition, the manner of administration and the like, which can readily be determined by one of ordinary skill in the art.
25 The term "transfection" means the introduction of a nucleic acid, i.e., an expression vector, into a recipient cell, which in certain instances involves nucleic acid-mediated gene transfer. The term "transformation" refers to a process in which a cell's genotype is changed as a result of the cellular uptake of exogenous nucleic acid. For example, a transformed cell may 3o express a recombinant form of a polypeptide of the presently disclosed subject matter or antisense expression may occur from the transferred gene so that the expression of a naturally occurring form of the gene is disrupted.

The term "transgene" means a nucleic acid sequence, which is partly or entirely heterologous to a transgenic animal or cell into which it is introduced, or, is homologous to an endogenous gene of the transgenic animal or cell into which it is introduced, but which is designed to be 5 inserted, or is inserted, into the animal's genome in such a way as to alter the genome of the cell into which it is inserted (i.e., it is inserted at a location which differs from that of the natural gene or its insertion results in a knockout). A transgene may include one or more regulatory sequences and any other nucleic acids, such as introns, that may be necessary for optimal expression.
The term "transgenic animal" refers to any animal, for example, a mouse, rat or other non-human mammal, a bird or an amphibian, in which one or more of the cells of the animal contain heterologous nucleic acid introduced by way of human intervention, such as by transgenic techniques ~s well known in the art. The nucleic acid is introduced into the cell, directly or indirectly, by way of deliberate genetic manipulation, such as by microinjection or by infection with a recombinant virus. The term genetic manipulation does not include classics! crossbreeding, or in vitro fertilization, but rather is directed to the introduction of a recombinant DNA
2o molecule. This molecule may be integrated vvithin a chromosome, or it may be extrachromosomaliy replicating DNA. In the typical transgenic animals described herein, the transgene causes cells to express a recombinant form of a protein. However, transgenic animals in which the recombinant gene is silent are also contemplated.
25 As used herein, the term "unit cell" refers to a basic parallelepiped shaped block. The entire volume of a crystal can be constructed by regular assembly of such blocks. Each unit cell comprises a complete representation of the unit of pattern, the repetition of which builds up the crystal. Thus, the term "unit cell" refers to the fundamental portion of a 3o crystal structure that is repeated infinitely by translation in three dimensions.
A unit cell is characterized by three vectors a, b, and c, not located in one plane, which form the edges of a parallelepiped. Angles a, ~, and y define the angles between the vectors: angle a is the angle between vectors b and c; angle ~ is the angle between vectors a and c; and angle y is the angle between vectors a and b. The entire volume of a crystal can be constructed by regular assembly of unit cells, each unit cell comprising a complete representation of the unit of pattern, the repetition of which builds up the s crystal.
The term "vector" refers to a nucleic acid capable of transporting another nucleic acid to which it has been linked. One type of vector that may be used in accord with the presently disclosed subject matter is an episome, i.e., a nucleic acid capable of extra-chromosomal replication. Other vectors ~o include those capable of autonomous replication and expression of nucleic acids to which they are linked. Vectors capable of directing the expression of genes to which they are operatively linked are referred to herein as "expression vectors". In general, expression vectors of utility in recombinant DNA techniques are often in the form of "plasmids" which refer to circular 15 double stranded DNA molecules that, in their vector form are not bound to the chromosome. In the present specification, "plasmid" and "vector" are used interchangeably as the plasmid is the most commonly used form of vector. However, the presently disclosed subject matter is intended to include such other forms of expression vectors which serve equivalent 2o functions and which become known in the art subsequently hereto.
Unless otherwise indicated, all numbers expressing quantities of ingredients, reaction conditions, and so forth used in the specification and claims are to be understood as being modified in all instances by the term "about". Accordingly, unless indicated to the contrary, the numerical 2s parameters set forth in this specification and attached claims are approximations that may vary depending upon the desired properties sought to be obtained by the presently disclosed subject matter.
1l. Description of Tables Table 1 presents data concerning the interfacial interactions in so PDE4D2-AMP. Table 1 includes data related to the atoms of individual amino acid residues and AMP that are predicted to be involved in the formation of either hydrogen bonds or van der Waals interactions.

Table 2 presents data concerning the predicted hydrogen bonding and van der Waals interactions that AMP makes with the active site residues of PDE4D2.
Table 3 presents statistics on diffraction data and structure refinement s of PDE4D2-AMP. See also Example 2.
Table 4 presents atomic structure coordinate data obtained from X-ray diffraction from the catalytic domain of PDE4D2 in complex with AMP.
Table 5 presents atomic structure coordinate data obtained from X-ray diffraction tram unligated PDE4D2 (polypeptide only without ligand).
1o III. Production of PDE4D2 Catalytic Domain Polyp_eptides The native and mutated PDE4D2 polypeptides, and fragments thereof, of the presently disclosed subject matter can be chemically synthesized in whole or part using techniques that are well known in the art (see i.e., Creighton, (1983) Proteins: Structures and Molecular Principles, 15 W.H. Freeman & Co., New York, incorporated herein in its entirety).
Alternatively, methods which are well known to those skilled in the art can be used to construct expression vectors containing a partial or the entire native or mutated PDE4D2 polypeptide coding sequence and appropriate transcriptional/translational control signals. These methods include in vitro 2o recombinant DNA techniques, synthetic techniques, and in vivo recombination/genetic recombination (see i.e., the techniques described throughout Sambrook et al., (1989) Molecular Cloningi: A Laborato~ Manual, Cold Spring Harbor Laboratory, New York, and Ausubel et al., (1989) Current Protocols in Molecular Biology, Greene Publishing Associates and 2s Wiley Interscience, New York, both incorporated herein in their entirety).
Some of the functions of a domain within the full-length protein are preserved when that particular domain is isolated from the remainder of the protein. Using conventional protein chemistry techniques, a modular domain can sometimes be separated from the parent protein. Using conventional 3o molecular biology techniques, each domain can usually be separately expressed with its original function intact or, as discussed herein below, chimeras comprising two different proteins can be constructed, wherein the chimeras retain the properties of the individual functional domains of the respective phosphodiesterases from which the chimeras were generated.
As described herein, the catalytic domain of a PDE4D2 can be expressed, crystallized, and its three dimensional structure determined with s a ligand bound as disclosed in the presently disclosed subject matter.
Additionally, the three dimensional structure that is determined can be used to identify new ligands and computational methods can be used to design ligands to its catalytic domain.
A variety of host-expression vector systems can be utilized to express ~o a PDE4D2 coding sequence. These include, but are not limited to microorganisms such as bacteria transformed with recombinant bacteriophage DNA, plasmid DNA or cosmid DNA expression vectors containing a PDE4D2 coding sequence; yeast transformed with recombinant yeast expression vectors containing a PDE4D2 coding sequence; insect cell ~s systems infected with recombinant virus expression vectors (i.e., baculovirus) containing a PDE4D2 coding sequence; plant cell systems infected with recombinant virus expression vectors (i.e., cauliflower mosaic virus, CaMV; tobacco mosaic virus, TMV; or transformed with recombinant plasmid expression vectors (i.e., Ti plasmid) containing a PDE4D2 coding 2o sequence; or animal cell systems. The expression elements of these systems vary in their strength and specificities.
Depending on the hostlvector system utilized, any of a number of suitable transcription and translation elements, including constitutive and inducible promoters, can be used in the expression vector. For example, 2s when cloning in bacterial systems, inducible promoters such as pL of bacteriophage ~,, plac, ptrp, ptac (ptrp-lac hybrid promoter), and the like can be used. When cloning in insect cell systems, promoters such as the baculovirus polyhedrin promoter can be used. When cloning in plant cell systems, promoters derived from the genome of plant cells, such as heat 3o shock promoters; the promoter for the small subunit of ribulose bisphosphate carboxylase (RtJBISCO); the promoter for the chlorophyll alb binding protein;
or from plant viruses (i.e., the 35S RNA promoter of CaMV; the coat protein promoter of TMV) can be used. When cloning in mammalian cell systems, promoters derived from the genome of mammalian cells (i.e., metallothionein promoter) or from mammalian viruses (i.e., the adenovirus late promoter; the vaccinia virus 7:5K promoter) can be used. In each of these systems, one of ordinary skill in the art will appreciate that other promoters can be used, and as such, the list presented is not intended to be exhaustive.
IV. Anal,~sis of Protein Properties IV.A. Analysis of Proteins by X-ray Crystallography Generally IV.A.1. X-ray Structure Determination Exemplary methods for obtaining the three dimensional structure of the crystalline form of a molecule or complex are described herein and, in view of this specification, variations on these methods will be apparent to those skilled in the art (see Ducruix and Geige 1992, Crystallization of Nucleic Acids and Proteins: A Practical Approach, IRL Press, Oxford, England).
~5 A variety of methods involving x-ray crystallography are contemplated by the presently disclosed subject matter. For example, the presently disclosed subject matter contemplates producing a crystallized polypeptide of the presently disclosed subject matter, or a fragment thereof, by: (a) introducing into a host cell an expression vector comprising a nucleic acid 2o encoding for a polypeptide of the presently disclosed subject matter, or a fragment thereof; (b) culturing the host cell in a cell culture medium to express the poiypeptide or fragment; (c) isolating the polypeptide or fragment from the cell culture; and (d) crystallizing the polypeptide or fragment thereof. Alternatively, the presently disclosed subject matter 2s contemplates determining the three dimensional structure of a crystallized polypeptide of the presently disclosed subject matter, or a fragment thereof, by: (a) crystallizing a polypeptide of the presently disclosed subject matter, or a fragment thereof, such that the crystals will diffract x-rays to a resolution of 3.5 A or better; and (b) analyzing the polypeptide or fragment by x-ray 3o diffraction to determine the three-dimensional structure of the crystallized polypeptide.
X-ray crystallography techniques generally require that the protein molecules be available in the form of a crystal. Crystals may be grown from a solution containing a purified polypeptide of the presently disclosed subject matter, or a fragment thereof (i.e., a stable domain), by a variety of conventional processes. These processes include, for example, batch, liquid, bridge, dialysis, vapour diffusion (i.e:, hanging drop or sitting drop 5 methods). See e.g., McPherson, 1982, Preparation and Analysis of Protein Crystals, John Wiiey, New York; McPherson, 1990, fur. J. Biochem. 189: 1-23; W eber. 1991, Adv. Protein Chem. 41: 1-36.
In certain embodiments, native crystals of the presently disclosed subject matter may be grown by adding precipitants to the concentrated ~o solution of the polypeptide. The precipitants are added at a concentration just below that necessary to precipitate the protein. Water may be removed by controlled evaporation to produce precipitating conditions, which are maintained until crystal growth ceases.
The formation of crystals is dependent on a number of different 15 parameters, including pH, temperature, protein concentration, the nature of the solvent and precipitant, as well as the presence of added ions or ligands to the protein. In addition, the sequence of the polypeptide being crystallized will have a significant affect on the success of obtaining crystals. Many routine crystallization experiments may be needed to screen ali these 2o parameters for the few combinations that might give crystal suitable for x-ray diffraction analysis (see e.g., Jancarik; J & Kim, S.H., J. Appl. Cryst. 1991 24: 409-411 ).
Crystallization robots may automate and speed up the work of reproducibly setting up large number of crystallization experiments. Once 2s some suitable set of conditions for growing the crystal are found, variations of the condition may be systematically screened in order to find the set of conditions which allows the growth of sufficiently large, single, well ordered crystals. In certain instances, a polypeptide of the presently disclosed subject matter is co-crystallized with a compound that stabilizes the ao polypeptide.
A number of methods are available to produce suitable radiation for x-ray diffraction. For example, x-ray beams may be produced by synchrotron rings where electrons (or positrons) are accelerated through an electromagnetic field while traveling at close to the speed of light. Because the admitted wavelength may also be controlled, synchrotrons may be used as a tunable x-ray source (Hendrickson WA, Trends Biochem Sci 2000 Dec;
25(12): 637-43). For less conventional Laue diffraction studies, polychromatic x-rays covering a broad wavelength window are used to observe many diffraction intensities simultaneously (Stoddard BL, Curr.
Opin. Struct Biol 1998 Oct; 8(5): 612-8). Neutrons may also be used for solving protein crystal structures (Gutberlet T, Heinemann U & Steiner M, Acta Crystallogr D 2001, 57: 349-54).
1o Before data collection commences, a protein crystal may be frozen to protect it from radiation damage. A number of different cryo-protectants may be used to assist in freezing the crystal, such as methyl pentanediol (MPD), isopropanol, ethylene glycol, glycerol, formats, citrate, mineral oil, or a low-molecular-weight polyethylene glycol (PEG). The presently disclosed ~s subject matter contemplates a composition comprising a polypeptide of the presently disclosed subject matter and a cryo-protectant. As an alternative to freezing the crystal, the crystal may also be used for diffraction experiments performed at temperatures above the freezing point of the solution. In these instances, the crystal may be protected from drying out by 2o placing it in a narrow capillary of a suitable material (generally glass or quartz) with some of the crystal growth solution included in order to maintain vapour pressure.
X-ray diffraction results may be recorded by a number of ways know to one of skill in the art. Examples of area electronic detectors include 2s charge coupled device detectors, multi-wire area detectors and phosphoimager detectors (Amemiya, Y, 1997, Methods in Enzymoloav, Vol.
276, Academic Press, San Diego, California, United States of America, pp.
233-243; Westbrook EM & Naday l, 1997, Methods in Enzymoloay, Vol. 276, Academic Press, San Diego, California, United States of America, pp. 244-30 268; Kahn R & i=ourme R, 1997, Methods in Enzymoloqy, Vol. 276, Academic Press, San Diego, California, United States of America, pp. 268-286).

A suitable system for laboratory data collection might include a Bruker AXS Proteum R system, equipped with a copper rotating anode source, Confocal MAX-FLUXT"" optics and a SMART 6000 charge coupled device detector. Collection of x-ray diffraction patterns are well documented by s those skilled in the art (see i.e., Ducruix and Geige, 1992, Crystallization of Nucleic Acids and Proteins: A Practical A~aproach, IRL Press, Oxford, England).
The theory behind diffraction by a crystal upon exposure to x-rays is well known. Because phase information is not directly measured in the diffraction experiment, and is needed to reconstruct the electron density map, methods that can recover this missing information are required. One method of solving structures ab initio are the real I reciprocal space cycling techniques. Suitable real / reciprocal space cycling search programs include shake-and-bake (Weeks CM, DeTitta GT, Hauptman HA, Thuman P, Miller 15 R, Acta Crystallogr A 1994; 50: 210-20).
Other methods for deriving phases may also be needed. These techniques generally rely on the idea that if two or more measurements of the same reflection are made where strong, measurable, differences are attributable to the characteristics of a small subset of the atoms alone, then 2o the contributions of other atoms can be, to a first approximation, ignored, and positions of these atoms may be determined from the difference in scattering by one of the above techniques. Knowing the position and scattering characteristics of those atoms, one may calculate what phase the overall scattering must have had to produce the observed differences.
2s One version of this technique is isomorphous replacement technique, which requires the introduction of new, well ordered, x-ray scatterers into the crystal. These additions are usually heavy metal atoms, (so that they make a significant difference in the diffraction pattern); and if the additions do not change the structure of the molecule or of the crystal cell, the resulting 3o crystals should be isomorphous. Isornorphous replacement experiments are usually performed by diffusing different heavy-metal metals into the channels of a pre-existing protein crystal. Growing the crystal from protein that has been soaked in the heavy atom is also possible (Petsko GA, 1985, Methods in Enz~qy, Vol. 114, Academic Press, Orlando, Florida, United States of America, pp. 147-156). Alternatively, the heavy atom may also be reactive and attached covalently to exposed amino acid side chains (such as the sulfur atom of cysteine) or it may be associated through non-covalent interactions. It is sometimes possible to replace endogenous light metals in metalio-proteins with heavier ones, i.e., zinc by mercury, or calcium by samarium (Petsko GA, 1985, Methods in Enzymology, Vol. 114, Academic Press, Orlando, Florida, United States of America, pp. 147-156). Exemplary sources for such heavy compounds include, without limitation, sodium ~o bromide, sodium selenate, trimethyl lead acetate, mercuric chloride, methyl mercury acetate, platinum tetracyanide, platinum tetrachloride, nickel chloride, and europium chloride.
A second technique for generating differences in scattering involves the phenomenon of anomalous scattering. X-rays that cause the 15 displacement of an electron in an inner shell to a higher shell are subsequently rescattered, but there is a time lag that shows up as a phase delay. This phase delay is observed as a (generally quite small) difference in intensity between reflections known as Friedel mates that would be identical if no anomalous scattering were present. A second effect related to 2o this phenomenon is that differences in the intensity of scattering of a given atom will vary in a wavelength dependent manners given rise to what are known as dispersive differences. In principle anomalous scattering occurs with all atoms, but the effect is strongest in heavy atoms, and may be maximized by using x-rays at a wavelength where the energy is equal to.the 2s difference in energy between shells. The technique therefore requires the incorporation of some heavy atom much as is needed for isomorphous replacement, although for anomalous scattering a wider variety of atoms are suitable, including lighter metal atoms (copper, zinc, iron) in metallo-proteins.
One method 'for preparing a protein for anomalous scattering involves so replacing the methionine residues in whole or in part with selenium containing seleno-methionine. Soaks with halide salts such as bromides and other non-reactive ions may also be effective (Dauter Z, Li M, Wlodawer A., Acta Crystallogr D 2001; 57: 239-49).

In another process, known as multiple anomalous scattering or MAD, two to four suitable wavelengths of data are collected. (Hendrickson WA &
Ogata CM, 1997, Methods in Enz~olorqy, Vol. 276, San Diego, California, United States of America, pp. 494-523}. Phasing by various combinations of s single and multiple isomorphous and anomalous scattering are possible too.
For example, SIRAS (single isomorphous replacement with anomalous scattering) utilizes both the isomorphous and anomalous differences for one derivative to derive phases. More traditionally, several different heavy atoms are soaked into different crystals to get sufficient phase information from ~o isomorphous differences while ignoring anomalous scattering, in the technique known as multiple isomorphous replacement (MIR) {Petsko GA, 1985, Methods in En~mology, Vol. 114, Academic Press, Orlando, Florida, United States of America, pp. 147-156).
Additional restraints on the phases may be derived from density modification techniques. These techniques use either generally known features of electron density distribution or known facts about that particular crystal to improve the phases. For example, because protein regions of the crystal scatter more strongly than solvent regions, solvent flattening/flipping may be used to adjust phases to make solvent density a uniform flat value 20 (Zhang KYJ, Cowtan K, & Main P, 1997, Methods in Enz~mology, Vol. 277, Academic Press, Orlando, Florida, United States of America, pp. 53-64). If more than one molecule of the protein is present in the asymmetric unit, the fact that the different molecules should be virtually identical may be exploited to further reduce phase error using non-crystallographic symmetry averaging 2s (Villieux FMD & Read RJ, 1997, Methods in Enzymologar, Vol. 277, Academic Press, Orlando, Florida, United States of America, pp. 18-52).
Suitable programs for performing these processes include DM and other programs of the CCP4 suite (Collaborative Computational Project, Number 4, 1994, Acta Cryst D50: 760-763) and CNX.
3o The unit cell dimensions, symmetry, vector amplitude and derived phase information can be used in a Fourier transform function to calculate the electron density in the unit cell, i.e., to generate an experimental electron density map. This may be accomplished using programs of the CNX or CCP4 packages. The resolution is measured in Angstrom (A) units, and is closely related to how far apart two objects need to be before they can be reliably distinguished. The smaller this number is, the higher the resolution and therefore the greater the amount of detail that can be seen. In 5 alternative embodiments, crystals of the presently disclosed subject matter diffract x-rays to a resolution of better than about 4.0, 3.5, 3.0, 2.5, 2.0, 1.5, 1.0, 0.5 A, or better.
As used herein, the term "modeling includes the quantitative and qualitative analysis of molecular structure andlor function based on atomic ~o structural information and interaction models. The term "modeling" includes conventional numeric-based molecular dynamic and energy minimization models, interactive computer graphic models, modified molecular mechanics models, distance geometry and other structure-based constraint models.
Model building may be accomplished by either the crystallographer 15 using a computer graphics program such as TURBO or O (Jones TA et al., 1991, Acta Crystaliogr. A47: 100-119) or, under suitable circumstances, by using a fully automated model building program, such as wARP (Perrakis A, Morris R, & Lamzin, VS, May 1999, Nature Structural Biology 6: 458-463) or MAID (Levitt DG, Acta Crystallogr. D 2001 57. 1013-9). This structure may 2o be used to calculate mode!-derived diffraction amplitudes and phases. The model-derived and experimental diffraction amplitudes may be compared and the agreement between them can be described by a parameter referred to as R-factor. A high degree of correlation in the amplitudes corresponds to a low R-factor value, with 0.0 representing exact agreement and 0.59 25 representing a completely random structure. Because the R-factor may be lowered by introducing more free parameters into the model, an unbiased, cross-correlated version of the R-factor known as the R-free gives a more objective measure of model quality. For the calculation of this parameter a subset of reflections (generally around 10%) are set aside at the beginning 30 of the refinement and not used as part of the refinement target. These reflections are then compared to those predicted by the model (Kleywegt GJ
& Brunger AT, Structure 1996 4(8): 897-904).

The model may be improved using computer programs that maximize the probability that the observed data was produced from the predicted model, while simultaneously optimizing the model geometry. For example, the CNX program may be used for model refinement, as can the XPLOR
s program (Murshudov GN, Vagin AA, & Dodson EJ, 1997, Acta Cryst. D Biol Crystaliogr 53: 247-255). In order to maximize the convergence radius of refinement, simulated annealing refinement using torsion angle dynamics may be employed in order to reduce the degrees of freedom of motion of the model (Adams PD, Pannu NS, Read RJ, Brunger AT, 1997, Proc Natl Acad to Sci U S A 94(10): 5018-23). Where experimental phase information is available (i.e., where MAD data was collected) Hendrickson-Lattman phase probability targets can be employed. Isotropic or anisotropic domain, group or individual temperature factor refinement, may be used to model variance of the atomic position from its mean. Well-defined peaks of electron density 1s not attributable to protein atoms are generally modeled as water molecules.
Water molecules may be found by manual inspection of electron density maps, or with automatic water picking routines. Additional small molecules, including ions, cofactors, buffer molecules, or substrates may be included in the model if sufficiently unambiguous electron density is observed in a map.
2o In general, the R-free is rarely as low as 0.15 and may be as high as 0.35 or greater for a reasonably well-determined protein structure. The residual difference is a consequence of approximations in the model (inadequate modeling of residual structure in the solvent, modeling atoms as isotropic Gaussian spheres, assuming all molecules are identical rather than 2s having a set of discrete conformers, etc.) and errors in the data (Lattman EE, 1996, Proteins 25: i-ii). In refined structures at high resolution, there are usually no major errors in the orientation of individual residues, and the estimated errors in atomic positions are usually around 0.1 - 0.2 up to 0.3 A.
The three dimensional structure of a new crystal may be modeled 3o using molecular replacement. The term "molecular replacement" refers to a method that involves generating a preliminary model of a molecule or complex whose structure coordinates are unknown, by orienting and positioning a molecule whose structure coordinates are known within the unit ceH of the unknown crystal, so as best to account for the observed diffraction pattern of the unknown crystal. Phases may then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This, in s turn, can be subject to any of the several forms of refinement to provide a final, accurate structure of the unknown crystal(Lattman E, 1985, Methods in Enzymoloq,Y, Vol. 115, pp. 55-77; Rossmann MG (ed.), 1972, The Molecular Replacement Method, Cordon & Breach, New York, New York, United States of America).
~o Commonly used computer software packages for molecular replacement are CNX, X-PLOR (Brunger 1992, Nature 355: 472-475), AMORE (Navaza, 1994, Acta Crystallogr. A50:157-163), the CCP4 package, the MERLOT package (Fitzgerald PMD, 1988 J. Appl. Cryst., Vol. 21, pp.
273-278) and XTALVIEW (McCree et al., 1992, J. AAoI. Graphics 10: 44-46).
~5 The quality of the model may be analyzed using a program such as PROCHECK or 3D-Profiler (Laskowski et al., 1993, J. AppG Cryst. 26:283-291; Luthy R et al., 1992, Nature 356: 83-85; and Bowie JU et al., 1991, Science 253: 164-170).
Homology modeling (also known as comparative modeling or 2o knowledge-based modeling) methods may also be used to develop a three dimensional model from a polypeptide sequence based on the structures of known proteins. The method utilizes a computer model of a known protein, a computer representation of the amino acid sequence of the polypeptide with an unknown structure, and standard computer representations of the 2s structures of amino acids. This method is well known to those skilled in the art (Greer, 1985, Science 228: 1055; Bundell et aL, 1988, Eur. J. Biochem.
172: 513; Knighton et aL, 1992, Science 258: 130-135, http:/lbiochem.vt.edulcourses/-modeling/homology.htn). Computer programs that can be used in homology modeling are QUANTA and the 3o Homology module in the Insight II modeling package distributed by Molecular Simulations Inc. (now part of Accelrys Inc., San Diego, California, United States of America), or MODELLER (Rockefeller University, New York, New York, United States of America; www.iucr.ac.uklsinris-top/logicallprg-modeller.html).
Once a homology model has been generated it is analyzed to determine its correctness. A computer program available to assist in this s analysis is the Protein Health module in QUANTA that provides a variety of tests. Other programs that provide structure analysis along with output include PROCHECK and 3D-Profiler (Luthy R et al., 1992, Nature 356: 83-85; and Bowie et al., 1991, Science 253: 164-170). Once any irregularities have been resolved, the entire structure may be further refined.
~o Other molecular modeling techniques may also be employed in accordance with presently disclosed subject matter. See e.g., Cohen et al., 1990, J. Med. Chem. 33: 883-894; Navia MA & Murcko MA, 1992, Current Opinions in Structural Biology 2: 202-210.
Under suitable circumstances, the entire process of solving a crystal ~s structure may be accomplished in an automated fashion by a system such as ELVES (http:llucxray.berkeley.edu/ jamesh/elveslindex.html) with little or no user intervention.
IV.A.2. X-ray Structure The presently disclosed subject matter provides methods for 2o determining some or all of the structural coordinates for amino acids of a polypeptide of the presently disclosed subject matter, or a complex thereof.
In another aspect, the presently disclosed subject matter provides methods for identifying a druggabie region of a polypeptide of the presently disclosed subject matter. For example, one such method includes:
25 (a) obtaining crystals of a polypeptide of the presently disclosed subject matter or a fragment thereof such that the three dimensional structure of the crystallized protein can be determined to a resolution of 3.5 A or better;
(b) determining the three dimensional structure of the crystallized polypeptide or fragment using x-ray diffraction; and (c) identifying a so druggable region of a polypeptide of the presently disclosed subject matter based on the three-dimensional structure of the polypeptide or fragment.
A three dimensional structure of a molecule or complex may be described by the set of atoms that best predict the observed diffraction data (that is, which possesses a minimal R value). Files may be created for the structure that defines each atom by its chemical identity, spatial coordinates in three dimensions, root mean squared deviation from the mean observed position and fractional occupancy of the observed position.
Those of skill in the art understand that a set of structure coordinates 5 for an protein, complex or a portion thereof, is a relative set of points that define a shape in three dimensions. Thus, it is possible that an entirely different set of coordinates could define a similar or identical shape.
Moreover, slight variations in the individual coordinates may have little affect on overall shape. Such variations in coordinates may be generated because of mathematical manipulations of the structure coordinates. For example, structure coordinates could be manipulated by crystallographic permutations of the structure coordinates, fractionalization of the structure coordinates, integer additions or subtractions to sets of the structure coordinates, inversion of the structure coordinates or any combination of the above.
~s Alternatively, modifications in the crystal structure due to mutations, additions, substitutions, andlor deletions of amino acids, or other changes in any of the components that make up the crystal, could also yield variations in structure coordinates. Such slight variations in the individual coordinates will have little affect on overall shape. If such variations are within an acceptable 2o standard error as compared to the original coordinates, the resulting three-dimensional shape is considered to be structurally equivalent. It should be noted that slight variations in individual structure coordinates of a polypeptide of the presently disclosed subject matter or a complex thereof would not be expected to significantly alter the nature of modulators that 2s could associate with a druggable region thereof. Thus, for example, a modulator that bound to the active site of a polypeptide of the presently disclosed subject matter would also be expected to bind to or interfere with another active site whose structure coordinates define a shape that falls within the acceptable error.
3o A crystal structure of the presently disclosed subject matter may be used to make a structural or computer model of the polypeptide, complex, or portion thereof. A model may represent the secondary, tertiary, andlor quaternary structure of the polypeptide, complex, or portion. The configurations of points in space derived from structure coordinates according to the presently disclosed subject matter can be visualized as, for example, a holographic image, a stereodiagram, a model, or a computer-displayed image, and the presently disclosed subject matter thus includes s such images, diagrams, or models.
IV.A.3. Structural Equivalents Various computational analyses can be used to determine whether a molecule or the active site portion thereof is structurally equivalent with respect to its three-dimensional structure, to all or part of a structure of a 1o polypeptide of the presently disclosed subject matter or a portion thereof.
For the purpose of presently disclosed subject matter, any molecule or complex or portion thereof, that has a root mean square deviation of conserved residue backbone atoms (N, Ca, C, O) of less than about 1.75 A, when superimposed on the relevant backbone atoms described by the reference structure coordinates of a polypeptide of the presently disclosed subject matter, is considered "structurally equivalent" to the reference molecule. That is to say, the crystal structures of those portions of the two molecules are substantially identical, within acceptable error. Alternatively, the root mean square deviation may be is less than about 1.50, 1.40, 1.25, 20 1.0, 0.75, 0.5 or 0.35 A.
The term "root mean square deviation" is understood in the art and means the square root of the arithmetic mean of the squares of the deviations. It is a way to express the deviation or variation from a trend or object.
25 in another aspect, the presently disclosed subject matter provides a scalable three-dimensional configuration of points, at least a portion of said points, and preferably all of said points, derived from structural coordinates of at least a portion of a polypeptide of the presently disclosed subject matter and having a root mean square deviation from the structure coordinates of 3o the polypeptide of the presently disclosed subject matter of less than 1.50, 1.40, 1.25, 1.0, 0.75, 0.5 or 0.35 A. In certain embodiments, the portion of a polypeptide of the presently disclosed subject matter is 25%, 33%, 50%, 66%, 75%, 85%, 90% or 95% or more of the amino acid residues contained in the polypeptide.
In another aspect, the presently disclosed subject matter provides a molecule or complex including a druggable region of a polypeptide of the 5 presently disclosed subject matter, the druggable region being defined by a set of points having a root mean square deviation of less than about 1.75 J~
from the structural coordinates for points representing (a) the backbone atoms of the amino acids contained in a druggable region of a polypeptide of the presently disclosed subject matter, (b) the side chain atoms (and ~o optionally the Ca atoms) of the amino acids contained in such druggable region, or (c) all the atoms of the amino acids contained in such druggable region. In certain embodiments, only a portion of the amino acids of a druggable region may be included in the set of points, such as 25%, 33°l°, 50%, 66%, 75%, 85%, 90% or 95% or more of the amino acid residues ~s contained in the druggable region. In certain embodiments, the root mean square deviation may be less than 1.50, 1.40, 1.25, 1.0, 0.75, 0.5, or 0.35 A.
In still other embodiments, instead of a druggable region, a stable domain, fragment, or structural motif is used in place of a druggable region.
IV.A.4. Machine Dis~la~s and Machine Readable Storage 2o Media The presently disclosed subject matter provides a machine-readable storage medium including a data storage material encoded with machine readable data which, when using a machine programmed with instructions for using said data, displays a graphical three-dimensional representation of 25 any of the molecules or complexes, or portions thereof, of presently disclosed subject matter. In another embodiment, the graphical three-dimensional representation of such molecule, complex or portion thereof includes the root mean square deviation of certain atoms of such molecule by a specified amount, such as the backbone atoms by less than 0.8 A. In so another embodiment, a structural equivalent of such molecule, complex, or portion thereof, maybe displayed. fn another embodiment, the portion may include a druggable region of the polypeptide of the presently disclosed subject matter.

According to one embodiment, the presently disclosed subject matter provides a computer far determining at least a portion of the structure coordinates corresponding to x-ray diffraction data obtained from a molecule or complex, wherein said computer includes: (a) a machine-readable data 5 storage medium comprising a data storage material encoded with machine-readable data, wherein said data comprises at least a portion of the structural coordinates of a polypeptide of the presently disclosed subject matter; (b} a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein said data ~o comprises x-ray diffraction data from said molecule or complex; (c) a working memory for storing instructions for processing said machine-readable data of (a) and (b); (d) a central-processing unit coupled to said working memory and to said machine-readable data storage medium of (a) and (b) fior performing a Fourier transform of the machine readable data of (a) and for ~5 processing said machine readable data of (b) into structure coordinates;
and (e) a display coupled to said central-processing unit for displaying said structure coordinates of said molecule or complex. In certain embodiments, the structural coordinates displayed are structurally equivalent to the structural coordinates of a polypeptide of the presently disclosed subject 20 matter.
In an alternative embodiment, the machine-readable data storage medium includes a data storage material encoded with a first set of machine readable data which includes the Fourier transform of the structure coordinates of a polypeptide of the presently disclosed subject matter or a 2s portion thereof, and which, when using a machine programmed with instructions for using said data, can be cornbined with a second set of machine readable data including the x-ray diffractian pattern of a molecule or complex to determine at least a portion of the structure coordinates corresponding to the second set of machine readable data.
3o For example, a system for reading a data storage medium may include a computer including a central processing unit (CPU), a working memory which can be, i.e., random access memory (RAM) or "core"
memory, mass storage memory (such as one or more disk drives or CD-ROM drives), one or more display devices (i.e., cathode-ray tube ("CRT") displays, light emitting diode (LED) displays, liquid crystal displays (LCDs), electroluminescent displays, vacuum fluorescent displays, field emission displays (FEDs), plasma displays, projection panels, etc.), one or more user s input devices (i.e., keyboards, microphones, mice, touch screens, etc.), one or more input lines, and one or mare output lines, all of which are interconnected by a conventional bidirectional system bus. The system may be a stand-alone computer, or may be networked (i.e., through local area networks, wide area networks, intranets, extranets, or the Internet) to other systems (i.e., computers, hosts, servers, etc.). The system may also include additional computer controlled devices such as consumer electronics and appliances.
Input hardware may be coupled to the computer by input lines and may be implemented in a variety of ways. Machine-readable data of ~5 presently disclosed subject matter maybe inputted via the use of a modem or modems connected by a telephone line or dedicated data line.
Alternatively or additionally, the input hardware may include CD-ROM drives or disk drives. In conjunction with a display terminal, a keyboard may also be used as an input device.
2o Output hardware may be coupled to the computer by output lines and may similarly be implemented by conventional devices. By way of example, the output hardware may include a display device for displaying a graphical representation of an active site of presently disclosed subject matter using a program such as C,~UANTA as described herein. Output hardware might also 25 include a printer, so that hard copy output may be produced, or a disk drive, to store system output for later use.
In operation, a CPU coordinates the use of the various input and output devices, coordinates data accesses from mass storage devices, accesses to and from working memory, and determines the sequence of so data processing steps. A number of programs may be used to process the machine-readable data of presently disclosed subject matter. Such programs are discussed in reference to the computational methods of drug discovery as described herein. References to components of the hardware system are included as appropriate throughout the following description of the data storage medium.
Machine-readable storage devices useful in the presently disclosed subject matter include, but are not limited to, magnetic devices, electrical s devices, optical devices, and combinations thereof. Examples of such data storage devices include, but are not limited to, hard disk devices, CD
devices, digital video disk devices, floppy disk devices, removable hard disk devices, magneto-optic disk devices, magnetic tape devices, flash memory devices, bubble memory devices, holographic storage devices, and any other mass storage peripheral device. It should be understood that these storage devices include necessary hardware (i.e., drives, controllers, power supplies, etc.) as well as any necessary media (i.e., disks, flash cards, etc.) to enable the storage of data.
In one embodiment, the presently disclosed subject matter ~5 contemplates a computer readable storage medium comprising structural data, wherein the data include the identity and three-dimensional coordinates of a polypeptide of the presently disclosed subject matter or portion thereof. In another aspect, the presently disclosed subject matter contemplates a database comprising the identity and three-dimensional 2o coordinates of a polypeptide of the presently disclosed subject matter or a portion thereof. Alternatively, the presently disclosed subject matter contemplates a database comprising a portion or all of the atomic coordinates of a polypeptide of the presently disclosed subject matter or portion thereof.
25 IV.A.S. Structurally Similar Molecules and Complexes Structural coordinates for a polypeptide of the presently disclosed subject matter can be used to aid in obtaining structural information about another molecule or complex. This method of the presently disclosed subject matter allows determination of at least a portion of the three-so dimensional structure of molecules or molecular complexes that contain one or more structural features that are similar to structural features of a polypeptide of the presently disclosed subject matter. Similar structural features can include, for example, regions of amino acid identity, conserved active site or binding site motifs, and similarly arranged secondary structural elements (i.e., cc helices and ~ sheets). Many of the methods described above for determining the structure of a polypeptide of the presently disclosed subject matter may be used for this purpose as well.
5 For the presently disclosed subject matter, a "structural homolog" is a polypeptide that contains one or more amino acid substitutions, deletions, additions, or rearrangements with respect to the amino acid sequence of SEQ ID NOs: 2 or 4 or other polypeptide of the presently disclosed subject matter, but that, when folded into its native conformation, exhibits or is ~o reasonably expected to exhibit at least a portion of the tertiary (three-dimensional) structure of the polypeptide encoded by SEQ ID NOs: 2 or 4 or such other polypeptide of the presently disclosed subject matter. , For example, structurally homologous molecules can contain deletions or additions of one or more contiguous or noncontiguous amino acids, such as ~s a loop or a domain. Structurally homologous molecules also include modified polypeptide molecules that have been chemically or enzymatically derivatized at one or more constituent amino acids, including side chain modifications, backbone modifications, and N- and C-terminal modifications including acetylation, hydroxylation, methylation, amidation, and the 2o attachment of carbohydrate or lipid moieties, cofactors, and the like.
By using molecular replacement, all or part of the structure coordinates of a polypeptide of the presently disclosed subject matter can be used to determine the structure of a crystallized molecule or complex whose structure is unknown more quickly and efficiently than attempting to 2s determine such information ab initio. For example, in one embodiment presently disclosed subject matter provides a method of utilizing molecular replacement to obtain structural information about a molecule or complex whose structure is unknown including: (a) crystallizing the molecule or complex of unknown structure; (b) generating an x-ray diffraction pattern 3o from said crystallized molecule or complex; and (c) applying at least a portion of the structure coordinates for a polypeptide of the presently disclosed subject matter to the x-ray diffraction pattern to generate a three-dimensional electron density map of the molecule or complex whose structure is unknown.
In another aspect, the presently disclosed subject matter provides a method for generating a preliminary model of a molecule or complex whose s structure coordinates are unknown, by orienting and positioning the relevant portion of a polypeptide of the presently disclosed subject matter within the unit cell of the crystal of the unknown molecule or complex so as best to account for the observed x-ray diffraction pattern of the crystal of the molecule or complex whose structure is unknown.
~o Structural information about a portion of any crystallized molecule or complex that is sufficiently structurally similar to a portion of a polypeptide of the presently disclosed subject matter may be resolved by this method. In addition to a molecule that shares one or more structural features with a polypeptide of the presently disclosed subject matter, a molecule that has ~s similar bioactivity, such as the same catalytic activity, substrate specificity or ligand binding activity as a polypeptide of the presently disclosed subject matter, may also be sufficiently structurally similar to a polypeptide of the presently disclosed subject matter to permit use of the structure coordinates for a polypeptide of the presently disclosed subject matter to solve its crystal 2o structure.
In another aspect, the method of molecular replacement is utilized to obtain structural information about a complex containing a polypeptide of the presently disclosed subject matter, such as a complex between a modulator and a polypeptide of the presently disclosed subject matter (or a domain, 2s fragment, ortholog, homolog etc. thereof). In certain instances, the complex includes a polypeptide of the presently disclosed subject matter (or a domain, fragment, ortholog, homolog etc. thereof) co-complexed with a modulator. For example, in one embodiment, the presently disclosed subject matter contemplates a method for making a crystallized complex 3o comprising a polypeptide of the presently disclosed subject matter, or a fragment thereof, and a compound having a molecular weight of less than 5 kDa, the method comprising: (a) crystallizing a polypeptide of the presently disclosed subject matter such that the crystals will diffract x-rays to a resolution of 3.5 A or better; and (b) soaking the crystal in a solution comprising the compound having a molecular weight of less than 5 kDa, thereby producing a crystallized complex comprising the polypeptide and the compound.
5 Using homology modeling, a computer model of a structural homolog or other polypeptide can be built or refined without crystallizing the molecule.
For example, in another aspect, the presently disclosed subject matter provides a computer-assisted method for homology modeling a structural homolog of a polypeptide of the presently disclosed subject matter including:
~o aligning the amino acid sequence of a known or suspected structural homolog with the amino acid sequence of a pofypeptide of the presently disclosed subject matter and incorporating the sequence of the homolog into a model of a polypeptide of the presently disclosed subject matter derived from atomic structure coordinates to yield a preliminary model of the 15 homolog; subjecting the preliminary model to energy minimization to yield an energy minimized model; remodeling regions of the energy minimized model where stereochemistry restraints are violated to yield a final model of the homolog.
In another embodiment, the presently disclosed subject matter 2o contemplates a method for determining the crystal structure of a homofog of a polypeptide having SEQ ID NO: 2 or SEQ ID NO: 4, or equivalent thereof, the method comprising: (a) providing the three dimensional structure of a crystallized polypeptide having SEQ ID NO: 2 or SEQ ID NO: 4, or a fragment thereof; (b) obtaining crystals of a homologous polypeptide 25 comprising an amino acid sequence that is at least 80% identical to the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4 such that the three dimensional structure of the crystallized homologous polypeptide may be determined to a resolution of 3.5 A or better; and (c) determining the three dimensional structure of the crystallized homologous polypeptide by x-so ray crystallography based on the atomic coordinates of the three dimensional structure provided in step (a). In certain instances of the foregoing method, the atomic coordinates for the homologous polypeptide have a root mean square deviation from the backbone atoms of the polypeptide having SEQ ID NO: 2 or SEQ ID NO: 4, or a fragment thereof, of not more than 1.5 A for all backbone atoms shared in common with the homologous polypeptide and the polypeptide having SEQ ID NO: 2 or SEQ
ID NO: 4, or a fragment thereof.
s IV.2. Formation of PDE4D2 Catalytic Domain-Liaand Crystals The presently disclosed subject matter provides crystals of PDE4D2 catalytic domain (CD) in complex with the ligand. In one embodiment, the PDE4D2 catalytic domain polypeptide used to produce crystals has the amino acid sequence shown in SEQ ID N0:4. The crystals were obtained ~o using the methodology disclosed in the Examples. Briefly, the crystals were grown by vapor diffusion against a well buffer of 50 mM HEPES (pH 7.5), 15% PEG3350, 25% ethylene glycol, 5% methanol, and 5% DMSO at 4°C.
The protein drop was prepared by mixing 10 mM cAMP and 0.4 mM zinc sulfate with 15 mg/mL PDE4D2 in a storage buffer of 50 mM NaCI, 20 mM
~s Tris-HCI (pH 7.5), and 1 mM !~-mercaptoethanol for the crystallization. To saturate the CAMP binding, the crystals were soaked in a buffer of 50 mM
HEPES (pH 7.5), 20% PEG3350, 25% ethylene glycol, 0.4 mM zinc sulfate, and 50 mM cAMP at room temperature for 5 hours and then immediately dipped into liquid nitrogen. The PDE4D2 crystals, which can be native or 2o derivative crystals, have a space group symmetry P2~2~2~. In this embodiment, there are four PDE4D2 CD molecules in the asymmetric unit.
In this PDE4D2 crystalline form, the unit cell has dimensions of a = 99.2 A, b = 111.2 A, c = 159.7 A, and a = (i = y = 90°. This crystal form can be produced in various ratios of the protein-ligand solutions versus the same 25 well buffer, such as 1 p.1 to 1 p.1.
The native and derivative co-crystals comprising a PDE4D2 CD and a ligand disclosed in the presently disclosed subject matter can be obtained by a variety of techniques, including batch, liquid bridge, dialysis, vapor diffusion, and hanging drop methods (see i.e., McPherson, Preparation and 3o Analysis of Protein C stals, ,lohn Wiley, New York, 1982; McPherson, Eur J
Biochem 189:1-23, 1990; Weber, Adv Protein Chem 41:1-36, 1991 ). In representative embodiments, the vapor diffusian and hangirig drop methods are used fior the crystallization of PDE4D2 polypeptides and fragments thereof.
Native crystals of the presently disclosed subject matter can be grown by dissolving a substantially pure PDE4D2 polypeptide or a fragment thereof, and optionally a ligand, in an aqueous buffer containing a precipitant at a concentration just below that necessary to precipitate the protein. Water is removed by controlled evaporation to produce precipitating conditions, which are maintained until crystal growth ceases.
In one embodiment ofi the presently disclosed subject matter, native crystals are grown by vapor diffusion (See i.e., McPherson, Preaaration and Analysis of Protein Cr~tals, John Wiley, New York, 1982; McPherson, Eur.
J. Biochem 189:1-23, 1990). In this method, the polypeptide/precipitant solution is allowed to equilibrate in a closed container with a larger aqueous reservoir having a precipitant concentration optimal for producing crystals.
Generally, less than about 25 ~,L of PDE4D2 polypeptide solution is mixed with an equal volume of reservoir solution, giving a precipitant concentration about half that required for crystallization. This solution is suspended as a droplet underneath a coverslip, which is sealed onto the top of the reservoir.
The sealed container is allowed to stand until crystals grow. Crystals 2o generally form within two to seven days, and are thereafter suitable for data collection. Of course, those of skill in the art will recognize that the above-described crystallization procedures and conditions can be varied.
The presently disclosed subject matter also provides methods for generating a crystalline form comprising a phosphodiesterase 4D2 25 (PDE4D2) catalytic domain polypeptide. In one embodiment, the method comprises crystallizing the PDE4D2 catalytic domain polypeptide by vapor diffusion, whereby a crystalline form of a PDE4D2 catalytic domain polypeptide is generated. In one embodiment, the solution comprises 10-15 mg/mL PDE4D2 in a storage buffer of 50 mM NaCI, 20 mM Tris-HCI (pH
so 7.5), and 1 mM f3-mercaptoethanol. In one embodiment, the crystalline form is grown by vapor diffusion against a well buffer comprising 100 mM HEPES
(pH 7.5), 16% PEG3350, 25% ethylene glycol, 10% methanol, and 10%

DMSO. In one embodiment, the crystalline form is grown at 4°C. (This is the crystallization condition for the unligated form of PDE4D2) The presently disclosed subject matter also provides methods for generating a crystalline form comprising a phosphodiesterase 4D2 s (PDE4D2) catalytic domain polypeptide in complex with a ligand. In one embodiment, the method comprises (a) incubating a solution comprising a phosphodiesterase 4D2 (PDE4D2) catalytic domain and a ligand; and (b) crystallizing the phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide and ligand by vapor diffusion, whereby a crystalline form of a phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide in complex with a ligand is generated. In one embodiment, the solution comprises 10 mM cAMP, 0.4 mM zinc sulfate, 15 mglmt_ PDE4D2 in a storage buffer of 50 mM NaCI, 20 mM Tris-HCI (pH 7.5), and 1 mM (3-mercaptoethanol. In one embodiment, the crystalline form is grown by vapor diffusion against a well ~5 buffer comprising 50 mM HEPES (pH 7.5), 15% PEG3350, 25% ethylene glycol, 5% methanol, and 5% DMSO. In one embodiment, the crystalline form is grown at 4°C.
This method is applicable to various iigands of PDE4D2 including, but not limited to CAMP. In certain embodiments, it is advantageous to saturate 2o the PDE4D2 binding sites with ligand. In one embodiment, the method further comprises saturating cAMP binding by soaking the crystalline form in a buffer of 50 mM HEPES (pH 7.5), 20% PEG3350, 25% ethylene glycol, 0.4 mM zinc sulfate, and 50 mM cAMP. This saturation step can be performed under various conditions. In one embodiment, the saturating occurs at room 2s temperature.
The presently disclosed subject matter also provides for a crystalline form produced by the methods.
V. Solving a Crystal Structure of the Presently disclosed su Ject matter Crystal structures of the presently disclosed subject matter can be so solved using a variety of techniques including, but not limited to isomorphous replacement, anomalous scattering, or molecular replacement methods.
Computer software packages can also be used to solve a crystal structure of the presently disclosed subject matter. Applicable software packages include, but are not limited to X-PLORT~ program (Brunger, 1992; available from Accelrys Inc, San Diego, California, United States of America), Xtal View (McRee, J Mol Graphics 10: 44-47, 1992; available from the San Diego Supercomputer Center, San Diego, California, United States of America);
s SHELXS 97 (Sheldrick, Acta Cryst, A46: 467, 1990; available from the Institute of Inorganic Chemistry, Georg-August-Universitat, Gottingen, Germany); SOLVE (Terwilliger, T.C. and J: Berendzen. Acta Crystallographica D55:849-861, 1999; see www.solve.lanl.gov) and SHAKE-AND-BAKE (Hauptman, Curr Opin Struct Biol 7: 672-80, 1997; Weeks et al., ~o Acta Cryst D49: 179, 1993; available from the Hauptman-Woodward .Medical Research Institute, Buffalo, New York, United States of America). See also, Ducruix & Geige, Crystallization of Nucleic Acids and Proteins: A Practical Approach, IRL Press, Oxford, England, 1992, and references cited therein.
In one embodiment, the structure of PDE4D2 in complex with AMP is ~s solved by the direct application of the tetramer of the PDE4D2-rolipram structure to the crystal system (Huai et al., 2003). The orientation of the individual subunits in the PDE4D2-AMP tetramer is optimized by rigid-body refinement of the Crystallography and NMR System (CNS; Brunger, 1998;
see http:Ilcns.csb.yale.edulv1.0/). The electron density map is improved by 20 the density modification package of CCP4 (1994). The atomic model is rebuilt by program O (Jones et al., 1991 ) and refined by CNS. See Table 3 for a summary of the statistics of the structure solved in this embodiment. In one embodiment, the three-dimensional structure of the crystallized complex can be determined to a resolution of about 2.3 A or better.
2s VI. Overall Structure of PDE4D2 Complex In one embodiment, the presently disclosed subject matter provides a binding site in a human PDE4D2 catalytic domain polypeptide for a substrate, wherein the substrate is in van der Waals, hydrogen bonding, or both van der Waals and hydrogen bonding contact with at least one of the so following residues of the human PDE4D2 polypeptide: Tyr159, His160, His164, His200; Asp201, Met273, Asp318, Leu319, Asn321, Thr333, I1e336, Phe340, G1n369, and Phe372. In one embodiment, the binding site comprises four PDE4D2 catalytic domain polypeptides. In another embodiment, at least two of the four PDE4D2 catalytic domain polypeptides are in van der Waals, hydrogen bonding, or both van der Waal and hydrogen bonding contact through at least one of the following residues: Arg116, Met147, Thr148, Asp151, Asn214, Thr215, Asn216, GIu218, AIa220, 5 Leu221, Met222, Tyr223, Asn224, Asp225, Asn231, Leu234, A1a235, Lys239, GIn242, GIu243, GIu244, Lys254, Arg257, G1n258, Arg261, I1e265, Arg346, GIu349, and Arg350.
VI.A. The Tetrameric Structure of the PDE4D2 Catalytic Domain The monomer of the catalytic domain of PDE4D2 with amino acids ~0 79-438 complexed with AMP contains sixteen alpha helices and possesses the same folding as that of PDE4B (Xu et al., 2000). fn one embodiment, four molecules of the PDE4D2 catalytic domains are tightly associated into a tetramer in the crystal (Figure 1 ), in comparison to a monomeric form in the PDE4B crystal. The electron density was excellent for the most amino acids ~s of PDE4D2, except that residues 412-438 were not traceable and presumably existed in a random conformation. In contrast, residues 496-508 of PDE4B that correspond to residues 422-434 of PDE4D2 showed a helix conformation. The different oligomerization status and the conformational differences at the C-terminus between PDE4D and PDE4B could imply 2o potential variations on the regulation of the catalysis by the PDE4 subfamilies.
The formation of the PDE4D2 tetramer is dominated by hydrogen bonds (Table 1, Figure 1). Helices H8 to H11 form the intertaces between subunits A and B or C and D. Helices H3, H8, H10, and H14 interact with 2s one another to form the interfaces between subunits A and C or B and D.
Subunit A also crossly contacts with subunit D via helix H11, so does subunit B with C (Table 1 ). The C-terminal residues after 412 of PDE4D2 were not traceable in the electron density of the crystals. However, the position of helix H16 (residues 392 tv 410) would predict that the C-terminus points 30 outside of the tetrameric body, implying their potential roles in the regulation of the catalysis, instead of dimerization. This view is different from the early thought of a dimerization rote of the C-terminus of PDE4 (Mehats et al., 2002). An indirect support to the regulation role of the C-terminus comes from the observation that the C-terminal helix 496-508 interacts with the active site via the crystallographic symmetry in the PDE4B structure (Xu et al., 2000).
The superposition of the PDE4D2 subunits in the tetramer shows an 5 average RMS deviation of 0.59 A for the backbone atoms of the four subunits, indicating the overall structural similarity among the subunits.
However, significant variations on local conformations are observed for certain loops in the PDE4D tetramer. A migration up to 3.4 A, about 5 times the average, was observed for the backbone atoms of loop Va1292 -~o Leu298. Since this loop is located far away from the active site of the enzyme, the conformational change of the loop might impact indirectly, if any, in the catalysis. In addition, the N-terminal residues 79-86 showed different conformations between subunits A and D, as revealed by their electron density. In contrast, no observable electron density for residues 79-15 86 of subunits B and C implies their random conformation. Finally, the averaged B-factors of 58.3 and 55.2 A2 for subunits B and C are significantly higher than 45.9 and 42.2 A2 for subunits A and D, indicating the relative conformation flexibility of subunits B and C. While it is not desired to be bound by any particular theory of operation, the interpretation to the 2o conformational variations in the PDE4D2 tetramer could imply an allosteric regulation of the PDE4 catalysis.
VLB. AMP Binding Referring now to Figure 2, the electron density revealed occupation of the reaction product 5'-AMP in the active site of PDE4D2 in spite of that 25 cAMP was used in the crystallization. The phosphate group of AMP directly interacts with both metal ions and forms the hydrogen bonds with His160, Asp201, and Asp318 (Table 2). It is also in a distance range of 3.2 - 4.0 A to residues Tyr159, His164, and His200. The adenosine group of AMP takes an anti conformation and orients to the hydrophobic pocket made up of 3o residues Tyr159, Leu319, Asn321, Thr333, I1e336, GIn369, and Phe372. It forms three hydrogen bonds with GIn369 and Asn321 and stacks against Phe372. The ribose of AMP has a configuration of C3' endo puckering and makes van der Waals' contacts with PDE residues His160, Met273, Asp318, Leu319, 1ie336, Phe340, and Phe372.
Mutations of the residues His160, His164, His200, Thr333, 11e336, Phe340, and Phe372 in the PDE4 subfamilies reduced or even abolished the s catalytic activity (Jin et al., 1992; Pillai et al., 1993; Jacobitz et al., 1997;
Atienza et al., 1999; Richter et al., 2001; Dym et al: 2002). It is also interesting to note that mutations on the corresponding AMP binding residues in other PDE families dramatically reduced the catalytic activity.
For example, the mutations on the PDE3A residues Tyr751 (Tyr159 in ~o PDE4D2), Asp950 (Asp318), Phe972 (Phe340), and Phe1004 (Phe372) made 15-280 fold loss of the catalytic efficiency (Zhang et al., 2001 ). The mutation of GIu672 in bovine PDESA (GIu230 in PDE4D2), an absolutely conserved residue across the PDE families, showed a significant reduction on Kcat (Turko et al., 1998).
~5 VI.C. Metal Binding Two metal ions have been allocated to the active site of PDE4D2.
The (2Fo-Fc) map revealed two strongest peaks: ~10s for the first metal site and ~6s for the second site that separate by about 3.8 A away. Each metal ion forms six coordinations with protein residues or water molecules in a 2o distorted octahedral configuration. As indicated in Figure 3, the first metal coordinates with His164, His200, Asp201, Asp318, and two phosphate oxygen atoms of AMP. The second metal coordinates with Asp318, two phosphate oxygen atoms of AMP, and three bound water molecules.
The anomalous scattering experiments at the wavelength of the zinc 25 absorption edge showed a jump of absorption, suggesting existence of zinc ion in the crystals. The first metal site has been assigned as zinc for its tight association with four protein residues and two oxygen atoms of AMP. The assignment for the second metal is difficult because of its loose binding.
Zinc was used as the second metal in the structure refinement because the so crystallization buffer contained 0.4 mM zinc sulfate. However, the physiological metal for the catalysis is not clear. It could be magnesium or other divalent ions as suggested by biochemical study that zinc at 1 ' ~,M
concentration and other divalent metals such as Mg2+, Mn2+, Co2+, and Ni2+

at 1-10 mM concentration activate the catalysis by PDE (Hardman et al., 1971; Francis et al., 1994; Percival et al., 1997).
The first metal site was proposed to play both structural and catalytic roles because it conjoins the residues from the three subdomains of PDE4 and constitutes a physical component of the active site (Xu et al., 2000).
Indeed, the structure of PDE4D2-AMP revealed the first metal ion forms two hydrogen bonds with the phosphate group, thus confirming its catalytic role (Figure 3). The observation that both metals coordinate with the phosphate group of AMP suggests a binuclear mechanism in which the hydrolysis of cAMP/cGMP is jointly accomplished by two divalent metals. The binuclear catalysis in PDE is similar to the hydrolysis of phosphoester bonds by protein phosphatases such as calcineurin (Lohse et al., 1995; Huai et al., 2002).
The identification of the zinc ion in the crystal structure of PDE4D2-AMP is supported by the high degree of homology between two conserved HX3HX24_26E sequences of PDE and the zinc enzymes (Vallee and Auld, 1990). However, two HX3HX24_26E motifs jointly form a single pocket for binding of both metal ions in the crystal structures of PDE4B (Xu et al., 2000) and PDE4D2, instead of that each motif binds an individual metal ion as one would predict. On the other hand, the number of zinc atoms at the active 2o sites in the different PDE families is controversial: one Zn2+ site per monomer (Percival et al., 1997), two Zn2+ for V. Fischeri PDE (Callahan et al., 1995) and for PDE4A (Omburo et al., 1998), and three Zn2+ for PDES
(Francis et al., 1994). The crystal structures of PDE4D2 and PDE4B and the structure-based sequence alignment showed the absolute conservation of 25 the metal binding residues across the PDE families and unlikely existence of other pockets for additional metal binding. While it is not desired to be bound by a particular theory of operation, this suggests that the binuclear catalysis is a potential universal mechanism for all families of PDEs.
VI.D. Complexes of PDE4D2 with a Liqand so The presently disclosed subject matter also provides complexes of PDE4D2 with a ligand. In one embodiment, the presently disclosed subject matter provides a complex of a human PDE4D2 catalytic domain polypeptide and a substrate, wherein the substrate is in van der Waals, hydrogen bonding, or both van der Waals and hydrogen bonding contact with at least one of the following residues of the human phosphodiesterase 4D2 (PDE4D2) polypeptide: Tyr159, His160, His164, His200, Asp201, Met273, Asp318, Leu319, Asn321, Thr333, I1e336, Phe340, GIn369, and Phe372. In 5 another embodiment, the complex comprises four PDE4D2 catalytic domain polypeptides. In another embodiment, at least two of the four PDE4D2 catalytic domain polypeptides are in van der Waals, hydrogen bonding, or both van der Waal and hydrogen bonding contact through one or more of the following residues: Arg116, Met147, Thr148, Asp151, Asn214, Thr215, 1o Asn216, GIu218, A1a220, Leu221, Met222, Tyr223, Asn224, Asp225, Asn231, Leu234, A1a235, Lys239, GIn242, GIu243, GIu244, Lys254, Arg257, GIn258, Arg261, I1e265, Arg346, GIu349, and Arg350. In still another embodiment, the complex comprises a metal ion.
The presently disclosed subject matter also provides a crystal of the ~s complex. In one embodiment, the crystal has the following physical measurements: space group P2~2~2~; and unit cell a = 99.2 A; b = 111.2 A;
c = 159.7 A.
VI. E. A Putative Mechanism of the Catalysis The essence of hydrolysis of a phophoester bond contains a step of 2o nucleophilic attack by a water molecule or a hydroxide ion. The structural study of PDE4B suggested that a water molecule bridging two metals could be a candidate for the nucleophilic attack on the phosphorus atom (Xu et al.
2000). However, this water molecule is displaced by the phosphate oxygen in the PDE4D2-AMP structure and is thus unlikely to play a role in the 2s catalysis. The crystal structure of PDE4D2-AMP showed three water molecules that form hydrogen bonds with protein residues and phosphate group of AMP and can be the potential candidates for the catalysis. Water molecule W3 (Figure 3) is coordinated with the second metal ion and forms three hydrogen bonds respectively with side chain atom Oe2 of GIu230, 3o carbonyl oxygen of Thr271, and a phosphate oxygen of AMP. Water molecule W4 forms hydrogen bonds with carbonyl oxygen of Asp318, side chain atom O" of Tyr159, and a phosphate oxygen of AMP. Water molecule W5 forms hydrogen bonds with side chain atom Ne of His204 and a phosphate oxygen of AMP. While not wishing to be bound by any particular theory of operation, W4 and W5 might play roles in orientation of the phosphate group and stabilization of the leaving group, and water W3 is the most likely candidate to serve as a nucleophile to attack the phosphoester s bond. Thus, the phosphate group of cAMP at the ground state forms hydrogen bonds with His160 and the two metal ions. These hydrogen bonds can polarize the phosphodiester bond and make the phosphor atom partially positively charged. Water molecule W3, after being activated by the metal ion and GIu230, attacks the phosphorus atom, while His160 serves as a proton donor to 03' for the completion of the phosphodiester bond hydrolysis (Figure 4).
VIII. Rational Druq Design VIII.A. Generally Modulators to polypeptides of the presently disclosed subject matter 15 and other structurally related molecules, and complexes containing the same, may be identified and developed as set forth below and otherwise using techniques and methods known to those of skill in the art.
The presently disclosed subject matter contemplates making any molecule that is shown to modulate the activity of a polypeptide of the 2o presently disclosed subject matter.
In another embodiment, inhibitors, modulators of the subject polypeptides, or biological complexes containing them, can be used in the manufacture of a medicament for any number of uses, including, for example, treating any disease or other treatable condition of a patient 25 (including humans and animals), and particularly a disease caused by aberrant PDE regulation or activity.
VIII.A.1 Drug Design A number of techniques can be used to screen, identify, select, and design chemical entities capable of associating with polypeptides of the so presently disclosed subject matter, structurally homologous molecules, and other molecules. Knowledge of the structure for a polypeptide of the presently disclosed subject matter, determined in accordance with the methods described herein, permits the design and/or identification of molecules andlor other modulators which have a shape complementary to the conformation of a polypeptide of the presently disclosed subject matter, or more particularly, a druggable region thereof. It is understood that such techniques and methods may use, in addition to the exact structural 5 coordinates and other information for a polypeptide of the presently disclosed subject matter, structural equivalents thereof described above (including, for example, those structural coordinates that are derived from the structural coordinates of amino acids contained in a druggable region as described above).
The term "chemical entity", as used herein, refers to chemical compounds, complexes of two or more chemical compounds, and fragments of such compounds or complexes. In certain instances, it is desirable to use chemical entities exhibiting a wide range of structural and functional diversity, such as compounds exhibiting different shapes (i.e., flat aromatic rings(s), puckered aliphatic rings(s), straight and branched chain aliphatics with single, double, or triple bonds) and diverse functional groups (i.e., carboxylic acids, esters, ethers, amines, aldehydes, ketones, and various heterocyclic rings).
In one aspect, the method of drug design generally includes 2o computationally evaluating the potential of a selected chemical entity to associate with any of the molecules or complexes of the presently disclosed subject matter (or portions thereof). For example, this method may include the steps of (a) employing computational means to perform a fitting operation between the selected chemical entity and a druggable region of 2s the molecule or complex; and (b) analyzing the results of said fitting operation to quantify the association between the chemical entity and the druggable region.
A chemical entity may be examined either through visual inspection or through the use of computer modeling using a docking program such as 3o GRAM, DOCK, or AUTODOCK (Dunbrack et al., Folding & Design, 2: 27-42 (1997)). This procedure can include computer fitting of chemical entities to a target to ascertain how well the shape and the chemical structure of each chemical entity will complement or interfere with the structure of the subject polypeptide (Bugg et al., Scientific American, Dec 1993: 92-98; Vilest et al., TIPS, 16:67-74 (1995)). Computer programs may also be employed to estimate the attraction, repulsion, and steric hindrance of the chemical entity to a druggable region, for example. Generally, the tighter the fit (i.e., the lower the steric hindrance, and/or the greater the attractive force) the more potent the chemical entity will be because these properties are consistent with a tighter binding constant. Furthermore, the more specificity in the design of a chemical entity the more likely that the chemical entity will not interfere with related proteins, which may minimize potential side-effects due ~o to unwanted interactions.
A variety of computational methods for molecular design, in which the steric and electronic properties of druggable regions are used to guide the design of chemical entities, are known: see e.g.; Cohen et al., 1990, J. Med.
Chem. 33: 883-894; Kuntz et al., 1982, J. Mol. 8iol 161: 269-288; DesJarlais 1988, J. Med. Chem. 31: 722-729; Bartlett et al., 1989, Spec. Publ., Roy.
Soc. Chem. 78: 182-196; Goodford et al., 1985, J. Med. Chem. 28: 849-857;
DesJarlais et a1.,1986, J. Med. Chem. 29: 2149-2153. Directed methods generally fall into two categories: (1 ) design by analogy in which 3-D
structures of known chemical entities (such as from a crystallographic 20 database) are docked to the druggable region and scored for goodness-of-fit; and (2) de novo design, in which the chemical entity is constructed piece-wise in the druggable region. The chemical entity may be screened as part of a library or a database of molecules. Databases which can be used include ACD (MDL Systems Inc., San Leandro, California, United States of 2s America), NCI (National Cancer Institute, Bethesda, Maryland, United States of America), CCDC (Cambridge Crystallographic Data Center, Cambridge, England, United Kingdom), CAST (Chemical Abstract Service), Derwent (Derwent Information Limited, London, England, United Kingdom), Maybridge (Maybridge Chemical Company Ltd., Cornwall, England, United ao Kingdom), Aldrich (Aldrich Chemical Company, St. Louis, Missouri, United States of America), DOCK (University of California in San Francisco, San Francisco, California, United States of America), and the Directory of Natural Products (Chapman & Hall). Computer programs such as CONCORD

(Tripos Inc., St. Louis, Missouri, United States of America) or DB-Converter (Molecular Simulations Limited, Cambridge, England, United Kingdom) can be used to convert a data set represented in two dimensions to one represented in three dimensions.
s Chemical entities may be tested for their capacity to fit spatially with a druggable region or other portion of a target protein. As used herein, the term "fits spatially" means that the three-dimensional structure of the chemical entity is accommodated geometrically by a druggable region. A
favorable geometric fit occurs when the surface area of the chemical entity is ~o in close proximity with the surface area of the druggable region without forming unfavorable interactions. A favorable complementary interaction occurs where the chemical entity interacts by hydrophobic, aromatic, ionic, dipolar, or hydrogen donating and accepting forces. Unfavorable interactions may be steric hindrance between atoms in the chemical entity ~s and atoms in the druggable region.
If a model of the presently disclosed subject matter is a computer model, the chemical entities may be positioned in a druggable region through computational docking. If, on the other hand, the model of the presently disclosed subject matter is a structural model, the chemical entities 2o may be positioned in the druggable region by, for example, manual docking.
As used herein the term "docking" refers to a process of placing a chemical entity in close proximity with a druggable region, or a process of finding low energy conformations of a chemical entity/druggable region complex.
In an illustrative embodiment, the design of potential modulator begins 25 from the general perspective of shape complimentary for the druggable region of a polypeptide of the presently disclosed subject matter, and a search algorithm is employed which is capable of scanning a database of small molecules of known three-dimensional structure for chemical entities which fit geometrically with the target druggable region. Most algorithms of 3o this type provide a method for finding a wide assortment of chemical entities that are complementary to the shape of a druggable region of the subject polypeptide. Each of a set of chemical entities from a particular data-base, such as the Cambridge Crystallographic Data Bank (CCDB) (Allen et al., 1973, J. Chem. Doc. 13: 119), is individually docked to the druggable region of a polypeptide of the presently disclosed subject matter in a number of geometrically permissible orientations with use of a docking algorithm. In certain embodiments, a set of computer algorithms called DOCK, can be s used to characterize the shape of invaginations and grooves that form the active sites and recognition surfaces of the druggable region (Kuntz et al., 1982, J. MoL Blol 161: 269-288). The program can also search a database of small molecules for templates whose shapes are complementary to particular binding sites of a polypeptide of the presently disclosed subject ~o matter (DesJarlais et al., 1988, J Med Chem 31: 722-729).
The orientations are evaluated for goodness-of-fit and the best are kept for further examination using molecular mechanics programs, such as AMBER or CHARMM. Such algorithms have previously proven successful in finding a variety of chemical entities that are complementary in shape to a 15 druggable region.
Goodford (1985, J Med Chem 28:849-857) and Boobbyer et al. (1989, J Med Chem 32:1083-1094) have produced a computer program (GRID) that seeks to determine regions of high affinity for different chemical groups (termed probes) of the druggable region. GRID hence provides a tool for 2o suggesting modifications to known chemical entities that might enhance binding. It may be anticipated that some of the sites discerned by GRID as regions of high affinity correspond to "pharmacophoric patterns" determined inferentially from a series of known ligands. As used herein, a "pharmacophoric pattern" is a geometric arrangement of features of chemical 2s entities that is believed to be important for binding. Attempts have been made to use pharmacophoric patterns as a search screen for novel ligands (lakes et al., 1987 J Mol Graph 5:41-48; Brint et al., '1987, J Mol Graph 5:49-56; lakes et al., 1986, J Mol Graph 4:12-20).
Yet a further embodiment of the presently disclosed subject matter 3o utilizes a computer algorithm such as CLIX which searches such databases as CCDB for chemical entities which can be oriented with the druggable region in a way that is both sterically acceptable and has a high likelihood of achieving favorable chemical interactions between the chemical entity and the surrounding amino acid residues. The method is based on characterizing the region in terms of an ensemble of favorable binding positions for different chemical groups and then searching for orientations of the chemical entities that cause maximum spatial coincidence of individual s candidate chemical groups with members of the ensemble. The algorithmic details of CLIX is described in Lawrence et al., 1992, Proteins 12:31-41.
In this way, the efficiency with which a chemical entity may bind to or interfere with a druggable region may be tested and optimized by computational evaluation. For example, for a favorable association with a druggable region, a chemical entity must preferably demonstrate a relatively small difference in energy between its bound and fine states (i.e., a small deformation energy of binding). Thus, certain, more desirable chemical entities will be designed with a deformation energy of binding of not greater than about 10 kcal/mole, and more preferably, not greater than 7 kcal/mole.
~5 Chemical entities may interact with a druggable region in more than one conformation that is similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the energy of the free entity and the average energy of the conformations observed when the chemical entity binds to the target.
2o In this way, the presently disclosed subject matter provides computer-assisted methods for identifying or designing a potential modulator of the activity of a polypeptide of the presently disclosed subject matter including:
supplying a computer modeling application with a set of structure coordinates of a molecule or complex, the molecule or complex including at 25 least a portion of a druggable region from a polypeptide of the presently disclosed subject matter; supplying the computer modeling application with a set of structure coordinates of a chemical entity; and determining whether the chemical entity is expected to bind to the molecule or complex, wherein binding to the molecule or complex is indicative of potential modulation of the 3o activity of a poiypeptide of the presently disclosed subject matter.
In another aspect, the presently disclosed subject matter provides a computer-assisted method for identifying or designing a potential modulator to a polypeptide of the presently disclosed subject matter, supplying a computer modeling application with a set of structure coordinates of a molecule or complex, the molecule or complex including at least a portion of a druggable region of a polypeptide of the presently disclosed subject matter; supplying the computer modeling application with a set of structure s coordinates for a chemical entity; evaluating the potential binding interactions between the chemical entity and active site of the molecule or molecular complex; structurally modifying the chemical entity to yield a set of structure coordinates for a modified chemical entity, and determining whether the modified chemical entity is expected to bind to the molecule or complex, wherein binding to the molecule or complex is indicative of potential modulation of the polypeptide of the presently disclosed subject matter.
In one embodiment, a potential modulator can be obtained by screening a peptide library (Scott & Smith, 1990, Science, 249: 386-390;
~s Cwirla et al., 1990, Proc. Natl. Acad. Sci. USA, 87: 6378-6382; Devlin et al., 1990, Science, 249: 404-406). A potential modulator selected in this manner could then be systematically modified by computer modeling programs until one or more promising potential drugs are identified. Such analysis has been shown to be effective in the development of HIV protease inhibitors 20 (Lam et al., 1994, Science 263: 380-384; Wlodawer et al., 1993, Ann. Rev.
Biochem. 62: 543-585; Appelt, 1993, Perspectives in Drug Discovery and Design 1: 23-48; Erickson, 1993, Perspectives in Drug Discovery and Design 1: 109-128). Alternatively a potential modulator may be selected from a library of chemicals such as those that can be licensed from third parties, 2s such as chemical and pharmaceutical companies. A third alternative is to synthesize the potential modulator de novo.
For example, in certain embodiments, the presently disclosed subject matter provides a method for making a potential modulator for a polypeptide of the presently disclosed subject matter, the method including synthesizing 3o a chemical entity or a molecule containing the chemical entity to yield a potential modulator of a polypeptide of the presently disclosed subject matter, the chemical entity having been identified during a computer-assisted process including supplying a computer modeling application with a set of structure coordinates of a molecule or complex, the molecule or complex including at least one druggable region from a polypeptide of the presently disclosed subject matter; supplying the computer modeling application with a set of structure coordinates of a chemical entity; and determining whether s the chemical entity is expected to bind to the molecule or complex at the active site, wherein binding to the molecule or complex is indicative of potential modulation. This method may further include the steps of evaluating the potential binding interactions between the chemical entity and the active site of the molecule or molecular complex and structurally ~o modifying the chemical entity to yield a set of structure coordinates for a modified chemical entity, which steps may be repeated one or more times.
Once a potential modulator is identified, it can then be tested in any standard assay far the macromolecule depending of course on the macromolecule, including in high throughput assays. Further refinements to ~5 the structure of the modulator will generally be necessary and can be made by the successive iterations of any andlor all of the steps provided by the particular screening assay, in particular further structural analysis by i.e., 15N NMR relaxation rate determinations or x-ray crystallography with the modulator bound to the subject polypeptide. These studies may be 2o performed in conjunction with biochemical assays.
Once identified, a potential modulator may be used as a model structure, and analags to the compound can be obtained. The analogs are then screened for their ability to bind the subject polypeptide. An analog of the potential modulator might be chosen as a modulator when it binds to the 2s subject polypeptide with a higher binding affinity than the predecessor modulator.
In a related approach, iterative drug design is used to identify modulators of a target protein. Iterative drug design is a method for optimizing associations between a protein and a modulator by determining 3o and evaluating the three dimensional structures of successive sets of protein/modulator complexes. In iterative drug design, crystals of a series of protein/modulator complexes are obtained and then the three-dimensional structures of each complex is solved. Such an approach provides insight into the association between the proteins and modulators of each complex.
For example, this approach may be accomplished by selecting modulators with inhibitory activity, obtaining crystals of this new protein/modulator complex, solving the three dimensional structure of the complex, and s comparing the associations between the new protein/modulator complex and previously solved protein/modulator complexes. By observing how changes in the modulator affected the protein/modulator associations, these associations may be optimized.
In addition to designing and/or identifying a chemical entity to associate with a druggable region, as described above, the same techniques and methods may be used to design andlor identify chemical entities that either associate, or do not associate, with affinity regions, selectivity regions or undesired regions of protein targets. By such methods, selectivity for one or a few targets, or alternatively for multiple targets, from the same species 15 Or from multiple species, can be achieved.
For example, a chemical entity may be designed andlor identified for which the binding energy for one druggable region, i.e., an affinity region or selectivity region, is more favorable than that for another region, i.e., an undesired region, by about 20%, 30%, 50% to about 60% or more. It may 2o be the case that the difference is observed between {a) more than two regions, (b) between different regions (selectivity, affinity or undesirable) from the same target, (c) between regions of different targets, {d) between regions of homologs from different species, or (e) between other combinations. Alternatively, the comparison may be made by reference to 2s the Kd, usually the apparent Kd, of said chemical entity with the two or more regions in question.
In another aspect, prospective modulators are screened for binding to two nearby druggable regions on a target protein. For example, a modulator that binds a first region of a target polypeptide does not bind a second 3o nearby region. Binding to the second region can be determined by monitoring changes in a different set of amide chemical shifts in either the original screen or a second screen conducted in the presence of a modulator {or potential modulator) for the first region. From an analysis of the chemical shift changes, the approximate location of a potential modulator for the second region is identified. Optimization of the second modulator for binding to the region is then carried out by screening structurally related compounds (i.e., analogs as described above). When modulators for the first region and the second region are identified, their location and orientation in the ternary complex can be determined experimentally. On the basis of this structural information, a linked compound, i.e., a consolidated modulator, is synthesized in which the modulator for the first region and the modulator for the second region are linked. in certain embodiments, the two modulators are covalently linked to form a consolidated modulator. This consolidated modulator may be tested to determine if it has a higher binding affinity for the target than either of the two individual modulators. A consolidated modulator is selected as a modulator when it has a higher binding affinity for the target than either of the two modulators. Larger consolidated modulators can be ~s constructed in an analogous manner, i.e., linking three modulators which bind to three nearby regions on the target to form a multilinked consolidated modulator that has an even higher affinity for the target than the linked modulator. In this example, it is assumed that is desirable to have the modulator bind to all the druggable regions. However, it may be the case 2o that binding to certain of the druggable regions is not desirable, so that the same techniques may be used to identify modulators and consolidated modulators that show increased specificity based on binding to at least one but not all druggable regions of a target.
The presently disclosed subject matter provides a number of methods 2s that use drug design as described above. For example, in one aspect, the presently disclosed subject matter contemplates a method for designing a candidate compound for screening for inhibitors of a polypeptide of the presently disclosed subject matter, the method comprising: (a) determining the three dimensional structure of a crystallized polypeptide of the presently so disclosed subject matter or a fragment thereof; and (b) designing a candidate inhibitor based on the three dimensional structure of the crystallized polypeptide or fragment.

In another aspect, the presently disclosed subject matter contemplates a method for identifying a potential inhibitor of a polypeptide of the presently disclosed subject matter, the method comprising: (a) providing the three-dimensional coordinates of a polypeptide of the presently disclosed 5 subject matter or a fragment thereof; (b) identifying a druggable region of the polypeptide or fragment; and (c) selecting from a database at least one compound that comprises three dimensional coordinates which indicate that the compound may bind the druggable region; (d) wherein the selected compound is a potential inhibitor of a polypeptide of the presently disclosed ~o subject matter.
In another aspect, the presently disclosed subject matter contemplates a method for identifying a potential modulator of a molecule comprising a druggable region similar to that of SEQ ID NO: 2 or SEQ ID
NO: 4, the method comprising: (a) using the atomic coordinates of amino ~5 acid residues from SEQ ID NO: 2 or SEQ ID NO: 4, or a fragment thereof, ~
a root mean square deviation from the backbone atoms of the amino acids of not more than 1.5 A, to generate a three-dimensional structure of a molecule comprising a druggable region that is a portion of SEQ ID NO: 2 or SEQ ID
NO: 4; (b) employing the three dimensional structure to design or select the 2o potential modulator; (c) synthesizing the modulator; and (d) contacting the modulator with the molecule to determine the ability of the modulator to interact with the molecule.
In another aspect, the presently disclosed subject matter contemplates an apparatus for determining whether a compound is a 25 potential inhibitor of a polypeptide having SEQ ID NO: 2 or SEQ ID NO: 4, the apparatus comprising: (a) a memory that comprises: (i) the three dimensional coordinates and identities of the atoms of a polypeptide of the presently disclosed subject matter or a fragment thereof that form a druggable site; and (ii) executable instructions; and (b) a processor that is 3o capable of executing instructions to: (i) receive three-dimensional structural information for a candidate compound; (ii) determine if the three-dimensional structure of the candidate compound is complementary to the structure of the interior of the druggable site; and (iii) output the results of the determination.
In another aspect, the presently disclosed subject matter contemplates a method for designing a potential compound for the prevention or treatment of a disease or disorder, the method comprising: (a) providing the three dimensional structure of a crystallized polypeptide of the presently disclosed subject matter, or a fragment thereof; (b) synthesizing a potential compound for the prevention or treatment of a disease or disorder based on the three dimensional structure of the crystallized polypeptide or ~o fragment; (c) contacting a polypeptide of the presently disclosed subject matter or a PDE with the potential compound; and (d) assaying the activity of a polypeptide of the presently disclosed subject matter, wherein a change in the activity of the polypeptide indicates that the compound may be useful for prevention or treatment of a disease or disorder.
In another aspect, the presently disclosed subject matter contemplates a method for designing a potential compound for the prevention or treatment of a disease or disorder, the method comprising: (a) providing structural information of a druggable region derived from NMR
spectroscopy of a polypeptide of the presently disclosed subject matter, or a 2o fragment thereof; (b) synthesizing a potential compound for the prevention or treatment of a disease or disorder based on the structural information; (c) contacting a polypeptide of the presently disclosed subject matter or a PDE
with the potential compound; and (d) assaying the activity of a polypeptide of the presently disclosed subject matter, wherein a change in the activity of the 2s polypeptide indicates that the compound may be useful for prevention or treatment of a disease or disorder.
VIII.B. Methods of Designing PDE4D2 CD Ligand Compounds The present X-ray structure of PDE4D2 baund to AMP provides an accurate three-dimensional structure of the catalytic pocket of PDE4D2.
so Novel ligands can be designed to fit this specific pocket using a variety of computational methods, discussed below. Alternatively, known ligands can be docked into the catalytic pocket, using a variety of docking programs and algorithms. These docked structures can be examined graphically to suggest chemical modifications that would improve their fit to the pocket, or their binding to the pocket. Alternatively, known ligands can be complexed with the PDE4D2 protein and crystallized using the methods of presently disclosed subject matter, allowing the structure of the complex to be 5 determined by X-ray crystallography. The three dimensional structures can be examined graphically to suggest chemical modifications that would improve their fit to the pocket, or their binding to the pocket.
The present X-ray structure of PDE4D2 can also be used as a template to build a three-dimensional model of the inhibitor structure of other ~o PDE families. Specifically, various computer software programs can be used to design novel ligands that would fit the specific pocket in the model for PDE4D2. Docking calculations can be used to predict how known PDE4D2 inhibitors will bind to the catalytic pocket of PDE4D2. These predicted complex structures can then be examined by computer graphics to 1s suggest specific chemical modifications that would enhance the binding to the activated state of PDE4D2.
To be useful as a therapeutic agent, a chemical compound that acts through PDE4D2 must reduce PDE4D2 activity to an appropriate level in relevant tissues. In principle, this can be achieved by adjusting the PDE4D2 2o conformational equilibrium so that appropriate fractions of the PDE4D2 protein exist in the activated and inactivated states. This in turn can be achieved with ligands that bind almost exclusively to one or the other of the two major conformational states. The design of ligands that are selective for a specific conformational state is facilitated by consideration of how these 25 ligands might bind to each of the two conformational states. Binding modes can be obtained using docking calculations, and then examined graphically to suggest chemical modifications that would make binding to a particular conformational state either more favorable or less favorable. Iterative application of these techniques can yield ligands with the desired level of so selectivity for the particular conformational state of PDE4D2, thereby achieving the desired level of PDE4D2 activity. Ligands that can bind to both conformational states of the PDE4D2 protein can also be designed.
This is also facilitated by consideration of how the ligands might bind to each of the two conformational states, using the same approach as discussed above, but this time seeking chemical structures and chemical modifications that would permit binding to both conformational states.
The methods of presently disclosed subject matter can also be used 5 to suggest possible chemical modifications of a compound that might reduce or minimize its effect on PDE4D2. This approach may be useful in drug discovery projects aiming to find compounds that modulate the activity of some other target molecule, where modulation of PDE4D2 activity is an undesirable side effect. This approach is useful in engineering PDE4D2 ~o activity out of other, non-drug molecules. I~umans and other animals are exposed to a wide range of different chemical compounds, some of which might act on PDE4D2 in an undesirable manner. Such a compound could be complexed with PDE4D2 and crystallized using the methods of the presently disclosed subject matter. The structure could then be determined 15 by X-ray crystallography. Alternatively, the structure of the complex could be predicted computationally using molecular docking software. In this case, compounds that tend to activate PDE4D2 would be docked into a model or structure of the activated form of PDE4D2, whereas compounds that tend to reduce the activity of PDE4D2 would be docked into a model or structure of 2o an inactivated form of PDE4D2, such as the complex presented here.
Whether the structure is obtained by X-ray crystallography or computational methods, the structure would be examined by computer graphics to suggest chemical modifications that would minimize the tendency to bind to PDE4D2. For example, substituents could be introduced 2s onto the compound that would project into volume occupied by the PDE4D2 protein. Alternatively, a region of the molecule that binds to a lipophilic region of the PDE4D2 binding site could be modified to make it more polar, thus reducing its tendency to bind to PDE4D2. Alternatively, a polar group of the compound that makes a hydrogen bonding interaction with PDE4D2 so could be identified and modified to an alternative group that fails to make the hydrogen bond. Appropriate chemical modifications can be chosen such that the desirable properties and behavior of the compound would be retained.

The design of candidate substances, also referred to as "compounds"
or "candidate compounds", that bind to or inhibit PDE CD (for example, PDE4D2 CD) -mediated activity according to the presently disclosed subject matter generally involves consideration of two factors. First, the compound must be capable of chemically and structurally associating with a PDE CD.
Non-covalent molecular interactions important in the association of a PDE
CD with its substrate include hydrogen bonding, van der Waals interactions, and hydrophobic interactions. The interaction between an atom of a CD
amino acid and an atom of a CD ligand can be made by any force or attraction described in nature. Usually the interaction between the atom of the amino acid and the ligand will be the result of a hydrogen bonding interaction, charge interaction, hydrophobic interaction, van der Waals interaction, or dipole interaction. In the case of the hydrophobic interaction, it is recognized that this is not a per se interaction between the amino acid and ligand, but rather the usual result, in part, of the repulsion of water or other hydrophilic group from a hydrophobic surface. Reducing or enhancing the interaction of the CD and a ligand can be measured by calculating or testing binding energies, either computationally or using thermodynamic or kinetic methods known in the art.
2o Second, the compound must be able to assume a conformation that allows it to associate with a PDE CD. Although certain portions of the compound will not directly participate in this association with a PDE CD, those portions can still influence the overall conformation of the molecule.
This influence on conformation, in turn, can have a significant impact on 25 potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity or compound in relation to all or a portion of the binding site, i.e., the catalytic pocket or an accessory binding site of a PDE CD, or the spacing between functional groups of a compound comprising several chemical entities that directly so interact with a PDE CD.
Chemical modifications can enhance or reduce interactions of an atom of a CD amino acid and an atom of an CD ligand. Steric hindrance can be a common approach for changing the interaction of a CD binding pocket with an activation domain. Chemical modifications are introduced in one embodiment at C-H, C-, and C-OH positions in a ligand, where the carbon is part of the ligand structure that remains the same after modification is complete. In the case of C-H, C could have 1, 2, or 3 hydrogens, but usually s only one hydrogen will be replaced. The H or OH can be removed after modification is complete and replaced with a desired chemical moiety.
The potential binding effect of a chemical compound on a PDE4D2 catalytic domain can be analyzed prior to its actual synthesis and testing by the use of computer modeling techniques that employ the coordinates of a ~o crystalline PDE CD, for example a PDE4D2 CD polypeptide of the presently disclosed subject matter. If the theoretical structure of the given compound suggests insuff;cient interaction and association between it and a PDE CD, synthesis and testing of the compound is obviated. However, if computer modeling indicates a strong interaction, the molecule can then be ~s synthesized and tested for its ability to bind and modulate the activity of a PDE CD. In this manner, synthesis of unproductive or inoperative compounds can be avoided.
Interacting amino acids forming contacts with a ligand and the atoms of the interacting amino acids are usually 2 to 4 A away from the center of 2o the atoms of the ligand. Generally these distances are determined by computer as discussed herein and in McRee (McRee, Practical Protein Crystalloara~hv, Academic Press, New York, 1993). However distances can be determined manually once the three dimensional model is made. More commonly, the atoms of the ligand and the atoms of interacting amino acids 2s are 3 to 4 A apart. A ligand can also interact with distant amino acids, after chemical modification of the ligand to create a new ligand. Distant amino acids are generally not in contact with the ligand before chemical modification. A chemical modification can change the structure of the ligand to make as new ligand that interacts with a distant amino acid usually at 30 least 4.5 A away from the ligand. Distant amino acids rarely line the surface of the binding cavity for the ligand, as they are too far away from the ligand to be part of a pocket or surface of the binding cavity.

In one embodiment, the presently disclosed subject matter provides a method for designing a ligand of a PDE4D2 polypeptide, the method comprising (a) forming a complex of a compound bound to the PDE4D2 polypeptide; (b) determining a structural feature of the complex formed in (a);
s wherein the structural feature is of a binding site for the compound; and (c) using the structural feature determined in (b) to design a ligand of a PDE4D2 polypeptide capable of binding to the binding site of PDE4D2.
Optionally, a method for designing a ligand of a PDE4D2 polypeptide can further comprise using a computer-based model of the complex formed ~o in (a) in designing the ligand. In one embodiment, a compound designed or selected as binding to a PDE polypeptide (in one embodiment a PDE4D2 CD polypeptide) can be further computationally optimized so that in its bound state it would lack repulsive electrostatic interaction with the target polypeptide. Such non-complementary (i.e., electrostatic) interactions include repulsive charge-charge, dipole-dipole, and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the ligand and the polypeptide when the ligand is bound to a PDE CD make a neutral or favorable contribution to the enthalpy of binding.
In another embodiment, a method for designing a ligand of a PDE4D2 2o polypeptide comprises (a) selecting a candidate PDE4D2 ligand; (b) determining which amino acid or amino acids of a PDE4D2 polypeptide interact with the ligand using a three-dimensional model of a crystallized protein, the model comprising a PDE4D2 catalytic domain in complex with a ligand; (c) identifying in a biological assay for PDE4~D2 activity a degree to 2s which the ligand modulates the activity of the PDE4D2 polypeptide; (d) selecting a chemical modification of the ligand wherein the interaction between the amino acids of the PDE4D2 pofypeptide and the ligand is predicted to be modulated by the chemical modification; (e) synthesizing a ligand having the chemical modified to form a modified ligand; (f) contacting 3o the modified ligand with the PDE4D2 polypeptide; (g) identifying in a biological assay for PDE4D2 activity a degree to which the modified ligand modulates the biological activity of the PDE4D2 polypeptide; and (h) comparing the biological activity of the PDE4D2 polypeptide in the presence of modified ligand with the biological activity of the PDE4D2 polypeptide in the presence of the unmodified ligand, whereby a ligand of a PDE4D2 polypeptide is designed. In one embodiment, the PDE4D2 polypeptide is a human PDE4D2 polypeptide. In another embodiment, the PDE4D2 s polypeptide comprises the amino acid sequence of SEQ 1D N0:2. In another embodiment, the method further comprises repeating steps (a) through (f), if the biological activity of the PDE4D2 polypeptide in the presence of the modified ligand varies from the biological activity of the PDE4D2 polypeptide in the presence of the unmodified ligand.
~o The presently disclosed subject matter also provides methods for identifying ligands of PDE4D2. In one embodiment, a method for identifying a PDE4D2 ligand can comprise (a) providing atomic coordinates of a phosphodiesterase 4D2 (PDE4D2) catalytic domain in complex with a ligand to a computerized modeling system; and (b) modeling a ligand that fits ~s spatially into the binding site of the PDE4D2 catalytic domain td thereby identify a PDE4D2 ligand. In one embodiment, the PDE4D2 catalytic domain comprises the amino acid sequence of SEQ ID N0:4. In another embodiment, the method further comprises identifying in an assay for PDE4D2-mediated activity a modeled ligand that increases or decreases the 2o activity of the PDE4D2.
In another embodiment, the presently disclosed subject matter provides a method of identifying a PDE4D2 ligand that selectively binds a PDE4D2 polypeptide compared to other potypeptides, the method comprising: (a) providing atomic coordinates of a PDE4D2 catalytic domain 2s in complex with a ligand to a computerized modeling system; and (b) modeling a ligand that fits into the binding pocket of a PDE4D2 catalytic domain and that interacts with residues of a PDE4D2 catalytic domain that are conserved among PDE4D2 subtypes to thereby identify a PDE4D2 ligand that selectively binds a PDE4D2 polypeptide compared to other so polypeptides. In one embodiment, the PDE4D2 catalytic domain comprises the amino acid sequence shown in SEQ ID N0:4. In another embodiment, the method further comprises identifying in a biological assay for PDE4D2 activity a modeled ligand that selectively binds to said PDE4D2 and increases or decreases the activity of the PDE4D2.
One of several methods can be used to screen chemical entities or fragments for their ability to associate with a PDE CD and, more particularly, s with the individual binding sites of a PDE CD, such as a catalytic pocket or an accessory binding site. This process can begin by visual inspection of, for example, a catalytic pocket on a computer screen based on the PDE4D2 CD atomic coordinates disclosed in Tables 4 and 5. Selected fragments or chemical entities can then be positioned in a variety of orientations, or docked, within an individual binding site of a PDE4D2 CD as defined herein above. Docking can be accomplished using software programs such as those available under the trade names QUANTA''' (available from Accelrys lnc, San Diego, California, United States of America) and SYBYLT""
(available from Tripos, Inc., St. Louis, Missouri, United States of America), 15 followed by energy minimization and molecular dynamics with standard molecular mechanics force fields, such as CHARM (Brooks et al., J Comp Ghem, 8: 132, 1993) and AMBER 5 (Case et al., AMBER 5, University of California, San Francisco, 1997; Pearlman et al., Comput Phys Common, 91: 1-4.1, 1995 ).
2o Specialized computer programs can also assist in the process of selecting fragments or chemical entities. These include:
1. GRIDT"" program, version 17 (Goodford, J Med Chem, 28: 849-57, 1985), which is available from Molecular Discovery Ltd. of Oxford, United Kingdom;
25 2. MCSST"" program (Miranker & Karplus, Proteins, 11:29-34, 1991 ), which is available from Accelrys Inc, San Diego, California, United States of America;
3. AUTODOCKT"" 3.0 program (Goodsell & Olsen, Proteins, 8:195-202, 1990), which is available from the Scripps Research Institute, La Jolla, 3o California, United States of America;
4. DOCKT"' 4..0 program (Kuntz et al., J Mol 8iol, 161:269-88, 1982), which is available from the University of California, San Francisco, California, United States of America;

5. FLEX-XT"' program (See Rarey et al., J Comput Aid Mol Des, 10:41-54, 1996), which is available from Tripos, lnc. of St. Louis, Missouri, United States of America;
6. MVP program (Lambert, in Practical Application of Computer s Aided Drub Design, Charifson, ed. Marvel-Dekker, New York, pp. 243-303, 1997); and 7. LUDI'~"' program (Bohm, J Comput Aid Mol Des, 6: 61-78, 1992), which is available from Accelrys Inc, San Diego, California, United States of America.
Once suitable chemical entities or fragments have been selected, they can be assembled into a single compound or ligand. Assembly can proceed by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of a PDE4D2 CD complex, optionally in further corr~plex with a ligand. Manual model building using software such as QUANTAT"" or SYBYLT"" typically follows.
Useful programs to aid one of ordinary skill in the art in connecting the individual chemical entities or fragments include:
1. CAVEATT"' program (Bartlett et al., Special Pub., Royal Chem 2o Soc, 78:182-96, 1989), which is available from the University ofi California, Berkeley, California, United States of America;
2. 3D Database systems, such as MACCS-3DT"" system program, which is available from MDL Information Systems of San Leandro, California, United States of America. This area is reviewed in Martin, J Med Chem 25 35:2145-54, 1992; and 3. HOOKT'~' program (Eisen et al., Proteins, 19:199-221, 1994), which is available from Accelrys Inc, San Diego, California, United States of America.
Instead of proceeding to build a PDE CD polypeptide figand (in one so embodiment a PDE4D2 CD ligand) in a step-wise fashion one fragment or chemical entity at a time as described above, ligand compounds can be designed as a whole or de novo using the structural coordinates of a crystalline PDE4D2 CD polypeptide of the presently disclosed subject matter and either an empty binding site or optionally including some portions) of a known ligand(s). Applicable methods can employ the following software programs:
1. LUDIT"" program (Bohm, J Compuf Aid Mol Des, 6:61-78, 1992), s which is available from Accelrys Inc, San Diego, California, United States of America;
2. LEGENDT"" program (Nishibata & Itai, Tetrahedron, 47:8985); and 3. LEAPFROGT''", which is available from Tripos Associates of St.
Louis, Missouri, United States of America.
~o Other molecular modeling techniques can also be employed in accordance with presently disclosed subject matter. See i.e., Cohen et al., J
Med Chem, 33:883-94, 1990; Navia & Murcko, Curr Opin Struct Biol, 2:202-10, 1992; and U.S. Patent No. 6,008,033 to Abdel-Meguid, et al., all of which are incorporated herein by reference.
~s Once a compound has been designed or selected by the above methods, the efficiency with which that compound can bind to a PDE CD can be tested and optimized by computational evaluation. By way of a particular example, a compound that has been designed or selected to function as a PDE4D2 CD ligand can traverse a volume not overlapping that occupied by 2o the binding site when it is bound to its native ligand. Additionally, an effective PDE CD iigand can demonstrate a relatively small difference in energy between its bound and free states (i.e., a small deformation energy of binding). Thus, the most efficient PDE CD ligands can be designed with a deformation energy of binding of in one embodiment not greater than about 2s 10 kcallmole, and in another embodiment not greater than 7 kcalimofe. It is possible for PDE CD ligands to interact with the polypeptide in more than one conformation that is similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the energy of the free compound and the average energy of the conformations so observed when the ligand binds to the polypeptide.
A compound designed or selected as binding to a PDE CD
polypeptide (in one embodiment a PDE4D2 polypeptide, and in another embodiment a PDE4D2 CD polypeptide) can be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target polypeptide. Such non-complementary (i.e., electrostatic) interactions include repulsive charge-charge, dipole-dipole, and charge-dipole interactions. Specifically, the sum s of all electrostatic interactions between the ligand and the polypeptide when the figand is bound to a PDE CD preferably make a neutral or favorable contribution to the enthalpy of binding.
Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include:
1. GAUSSIAN 98T"", which is available from Gaussian, Inc. of Pittsburgh, Pennsylvania, United States of America;
2. AMBERT"" program, version 6.0, which is available from the University of California, San Francisco, California, United States of America;
15 3. QUANTAT"~ program, which is available from Accelrys Inc, San Diego, California, United States of America;
4. CHARMM~ program, which is available from Accelrys Inc, San Diego, California, United States of America; and 4. INSIGHT II~ program, which is available from Accelrys Inc, San 2o Diego, California, United States of America.
These programs can be implemented using a suitable computer system. Other hardware systems and software packages will be apparent to those skilled in the art after review of the disclosure of the presently disclosed subject matter presented herein.
25 Once a PDE CD modulating compound has been optimally selected or designed, as described above, substitutions can then be made in some of its atoms or side groups in order to improve or modify its binding properties.
Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity, and charge as so the original group. Components known in the art to alter conformation are avoided. Such substituted chemical compounds can then be analyzed for efficiency of fit to a PDE CD binding site using the same computer-based approaches described in detail above.

V111.C. Sterically Similar Compounds A further aspect of the presently disclosed subject matter is that sterically similar compounds can be formulated to mimic the key portions of a PDE4D2 CD structure. Such compounds are functional equivalents. The 5 generation of a structural functional equivalent can be achieved by the techniques of modeling and chemical design known to those of skill in the art and described herein. Modeling and chemical design of PDE4D2 and PDE4D2 CD structural equivalents can be based on the structure coordinates of a crystalline PDE4D2 CD polypeptide of the presently ~o disclosed subject matter. It will be understood that all such sterically similar constructs fall within the scope of the presently disclosed subject matter.
VIII.D. Desiqnina a PDE4D2 Modulator The presently disclosed subject matter also provides methods for designing PDE4D2 modulators. In one embodiment, a method of designing 15 a chemical compound that modulates the biological activity of a target PDE4D2 polypeptide comprises (a) obtaining three-dimensional structures for a catalytic domain (CD) of PDE4D2 bound to a ligand, and wherein the structures are selected from the group consisting of X-ray structures and computer generated models; (b) rotating and translating the three-2o dimensional structures as rigid bodies so as to superimpose corresponding backbone atoms of a core region of the PDE4D2 CD; (c) comparing the superimposed three-dimensional structures to identify volume near a catalytic pocket of the PDE CD that is available to a ligand in one or more structures, but not available to the ligand in one or more other structures;
(d) 2s designing a chemical compound that could occupy the volume in some of the complexed structures, but not in others; (e) synthesizing the designed chemical compound; and (f) testing the designed chemical compound in a biological assay to determine whether it acts as a ligand of PDE4D2 with a desired effect on PDE4D2 biological activities, whereby a ligand of a so PDE4D2 polypeptide is designed.
!n another embodiment, the present method further comprises designing a chemical compound by considering a known agonist of the PDE
CD and adding a substituent that protrudes into the volume identified in step (c) or that makes a desired interaction. For any this embodiment, the designing a chemical compound can further comprise using computer modeling software as discussed hereinabove.
in another embodiment, the presently disclosed subject matter also s provides a method of designing a ligand that selectively modulates the activity of a PDE4D2 polypeptide comprising (a) evaluating a three-dimensional structure of a crystallized PDE4D2 catalytic domain polypeptide in complex with a ligand; and (b) synthesizing a potential ligand based on the three-dimensional structure of the crystallized PDE4D2 catalytic polypeptide ~o in complex with a ligand, whereby a ligand that selectively modulates the activity of a PDE4D2 polypeptide is designed. In one embodiment, the PDE4D2 catalytic domain polypeptide comprises the amino acid sequence of SEQ ID N0:4. In another embodiment, the crystallized PDE4D2 catalytic domain pofypeptide is in an orthorhombic crystalline form. In another ~s embodiment, the three-dimensional structure of the crystallized PDE4D2 catalytic domain pofypeptide in complex with a ligand can be determined to a resolution of about 2.3 A or better.
Optionally, the present method can further comprise contacting a PDE4D2 catalytic domain polypeptide with the potential ligand and a ligand;
2o and assaying the PDE4D2 catalytic domain polypeptide for binding of the potential ligand, for a change in activity of fihe PDE4D2 catalytic domain polypeptide, or both.
The presently disclosed subject matter also provides a method for screening a plurality of compounds for a ligand of a PDE4D2 catalytic 2s domain polypeptide comprising (a) providing a library of test samples; (b) contacting a crystalline form comprising a PDE4D2 polypeptide in complex with a ligand with each test sample; (c) detecting an interaction between a test sample and the crystalline PDE4D2 polypeptide in complex with a ligand; (d) identifying a test sample that interacts with the crystalline 3o PDE4D2 polypeptide in complex with a ligand; and (e) isolating a test sample that interacts with the crystalline PDE4D2 polypeptide in complex with a ligand, whereby a plurality of compounds is screened for a ligand of a PDE4D2 catalytic domain polypeptide. In one embodiment, the PDE4D2 polypeptide comprises a PDE4D2 catalytic damain. In another embodiment, the PDE4D2 polypeptide is a human PDE4D2 polypeptide. In another embodiment, the PDE4D2 polypeptide comprises the amino acid sequence of SEQ fD N0:4. In one embodiment, the library of test samples is bound to s a substrate. In another embodiment, the library of test samples is synthesized directly on a substrate.
IX. PDE4D2 Polypeptides The generation of mutant and chimeric PDE4D2 polypeptides is also an aspect of the presently disclosed subject matter. A chimeric polypeptide ~o can comprise a PDE4D2 CD polypeptide or a portion of a PDE4D2 CD, (i.e.
a PDE4D2 CD) which is fused to a candidate polypeptide or a suitable region of the candidate polypeptide. Throughout the present disclosure it is intended that the term "mutant" encompass not only mutants of a PDE4D2 CD polypeptide but chimeric proteins generated using a PDE4D2 CD as ~s well. It is thus intended that the following discussion of mutant PDE4D2 CDs apply mutatis mutandis to chimeric PDE4D2 and PDE4D2 CD polypeptides and to structural equivalents thereof.
In accordance with the presently disclosed subject matter, a mutation can be directed to a particular site or combination of sites of a wild-type 2o PDE4D2 CD. For example, an accessory binding site or the binding pocket can be chosen for mutagenesis. Similarly, a residue having a location on, at or near the surface of the polypeptide can be replaced, resulting in an altered surface charge of one or more charge units, as compared to the wild-type PDE4D2 and. PDE4D2 CD. Alternatively, an amino acid residue in a 2s PDE4D2 or a PDE4D2 CD can be chosen for replacement based on its hydrophilic or hydrophobic characteristics.
Such mutants can be characterized by any one of several different properties as compared with the wild-type PDE4D2 CD. For example, such mutants can have an altered surface charge of one or more charge units, or 3o can have an increase in overall stability. Other mutants can have altered substrate specificity in comparison with, or a higher specific activity than, a wild type PDE4D2 or PDE4D2 CD.

PDE4D2 and PDE4D2 CD mutants of the presently disclosed subject matter can be generated in a number of ways. For example, the wild-type sequence of a PDE4D2 or a PDE4D2 CD can be mutated at those sites identified using presently disclosed subject matter as desirable for mutation s by employing oligonucleotide-directed mutagenesis or other conventional methods. Alternatively, mutants of a PDE4D2 or a PDE4D2 CD can be generated by the site-specific replacement of a particular amino acid with an unnaturally occurring amino acid. In addition, PDE4D2 or PDE4D2 CD
mutants can be generated through replacement of an amino acid residue, for 1o example, a particular cysteine or methionine residue, with selenocysteine or selenomethionine. This can be achieved by growing a host organism capable of expressing either the wild type or mutant polypeptide on a growth medium depleted of either natural cysteine or methionine (or both) but enriched in selenocysteine or selenomethionine (or both).
15 Mutations can be introduced into a DNA sequence coding for a PDE4D2 or a PDE4D2 CD using synthetic oligonucleotides. These oligonucleotides contain nucleotide sequences flanking the desired mutation sites. Mutations can be generated in the full-length DNA sequence of a PDE4D2 or a PDE4D2 CD or in any sequence coding for polypeptide 2o fragments of a PDE4D2 or a PDE4D2 CD.
According to the presently disclosed subject matter, a mutated PDE4D2 or PDE4D2 CD DNA sequence, produced by the methods described above; or any alternative methods known in the art, can be expressed using an expression vector. An expression vector, as is well 25 known to those of skill in the art, typically includes elements that permit autonomous replication in a host cell independent of the host genome, and one or more phenotypic markers for selection purposes. Either prior to or after insertion of the DNA sequences surrounding the desired PDE4D2 or PDE4D2 CD mutant coding sequence, an expression vector includes control 3o sequences encoding a promoter, operator, ribosome binding site, translation initiation signal, and, optionally, a repressor gene or various activator genes and a signal for termination. Where secretion of the produced mutant is desired, nucleotides encoding a "signal sequence" can be inserted prior to a PDE4D2 or a PDE4D2 CD mutant coding sequence. For expression under the direction of the control sequences, a desired DNA sequence is operatively finked to the control sequences; that is, the sequence has an appropriate start signal in front of the DNA sequence encoding the PDE4D2 s or PDE4D2 CD mutant, and the correct reading frame to permit expression of that sequence under the control of the control sequences and production of the desired product encoded by that PDE4D2 or PDE4D2 CD sequence.
Any of a wide variety of well-known available expression vectors can be used to express a mutated PDE4D2 ar PDE4D2 CD coding sequences of ~o presently disclosed subject matter. These include for example, vectors consisting of segments of chromosomal, non-chromosomal, and synthetic DNA sequences, such as known derivatives of SV40, known bacterial plasmids, i.e., plasmids from E. toll including colE1, pCR1, pBR322, pMB9 and their derivatives, wider host range plasmids, i.e., RP4, phage DNAs, i.e., ~5 derivatives of phage ?, i.e., NM 989, and other DNA phages, i.e., M13 and filamentous single stranded DNA phages, yeast plasmids and vectors derived from combinations of plasmids and phage DNAs, such as plasmids which have been modified to employ phage DNA or other expression control sequences. In one embodiment of the presently disclosed subject matter, a 2o vector amenable to expression in a pET-based expression system is employed. The pET expression system is available from Novagen, Inc.
(Madison, Wisconsin, United States of America).
In addition, any of a wide variety of expression control sequences -i.e. sequences that control the expression of a DNA sequence when 2s operatively linked to it - can be used in these vectors to express the mutated DNA sequences according to presently disclosed subject matter. Such useful expression control sequences, include, but are not limited to the early and late promoters of SV40 for animal cells; the lac system, the trp system, the TAC or TRC system, the major operator and promoter regions of phage 30 ~,, and the control regions of fd coat protein far E. toll; the promoter for 3-phosphoglycerate kinase or other glycolytic enzymes, the promoters of acid phosphatase, (for example, PhoS), and the promoters of the yeast a-mating factors for yeast; as well as other sequences known to control the expression of genes of prokaryotic or eukaryotic cells or their viruses, and various combinations thereof.
A wide variety of hosts can be employed for producing mutated PDE4D2. and PDE4D2 CD polypeptides according to presently disclosed s subject matter. These hosts include, for example, bacteria, such as E. coli, Bacillus, and Streptomyces; fungi, such as yeasts; animal cells, such as CHO and COS-1 cells; plant cells; insect cells, such as Sf9 cells; and transgenic host cells.
It should be understood that not all expression vectors and expression systems function in the same way to express mutated DNA sequences of presently disclosed subject matter, and to produce modified PDE4D2 and PDE4D2 CD polypeptides or PDE4D2 or PDE4D2 CD mutants. Neither do all hosts function equally well with the same expression system. One of skill in the art can, however, make a selection among these vectors, expression ~s control sequences and hosts without undue experimentation and without departing from the scope of presently disclosed subject matter. For example, an important consideration in selecting a vector will be the ability of the vector to replicate in a given host. The copy number of the vector, the ability to control that copy number, and the expression of any other proteins 2o encoded by the vector, such as antibiotic markers, should also be considered.
In selecting an expression control sequence, a variety of factors should also be considered. These include, for example, the relative strength of the system, its controllability and its compatibility with the DNA sequence 2s encoding a modified PDE4D2 or PDE4D2 CD polypeptide of presently disclosed subject matter, with particular regard to the formation of potential secondary and tertiary structures.
Hosts should be selected by consideration of their compatibility with the chosen vector, the toxicity of a modified PDE4D2 or PDE4D2 CD to 3o them, their ability to express mature products, their ability to fold proteins correctly, their fermentation requirements, the ease of purification of a modified PDE4D2 or PDE4D2 CD and safety. UVithin these parameters, one of skill in the art can select various vector/expression control systemlhost combinations that will produce useful amounts of a mutant PDE4D2 or PDE4D2 CD. A mutant PDE4D2 or PDE4D2 CD produced in these systems can be purified by a variety of conventional steps and strategies, including those used to purify the wild type PDE4D2 or PDE4D2 CD.
s Once a PDE4D2 CD mutations) has been generated in the desired location, such as an active site or dimerization site, the mutants can be tested for any one of several properties of interest. For example, mutants can be screened for an altered charge at physiological pH. This is determined by measuring the mutant PDE4D2 or PDE4D2 CD isoelectric ~o point (p1) and comparing the observed value with that of the wild-type parent.
Isoelectric point can be measured by gel-electrophoresis according to the method of Wellner (Wellner, Anal Chem. 43:597, 1971 ). A mutant PDE4D2 or PDE4D2 CD polypeptide containing a replacement amino acid located at the surface of the enzyme, as provided by the structural information of 15 presently disclosed subject matter, can lead to an altered surface charge and an altered p1.
IX.A. Generation of an Engineered PDE4D2 CD or PDE4D2 CD
Mutant In an embodiment of the presently disclosed subject matter, a unique 2o PDE4D2 or PDE4D2 CD polypeptide is generated. Such a mutant can facilitate purification and the study of the catalytic abilities of a PDE4D2 polypeptide.
As used in the following discussion, the terms "engineered PDE4D2", "engineered PDE4D2 LDB", "PDE4D2 mutant", and "PDE4D2 CD mutant"
2s refers to polypeptides having amino acid sequences which contain at least one mutation in the wild-type sequence. The terms also refer to PDE4D2 and PDE4D2 CD polypeptides which are capable of exerting a biological effect in that they comprise all or a part of the amino acid sequence of an engineered PDE4D2 or PDE4D2 CD polypeptide of the presently disclosed so subject matter, or cross-react with antibodies raised against an engineered PDE4D2 or PDE4D2 CD polypeptide, or retain all or some or an enhanced degree of the biological activity of the engineered PDE4D2 or PDE4D2 CD

amino acid sequence or protein. Such biological activity can include catalytic activity and the binding of small molecules in general.
The terms "engineered PDE4D2 CD" and "PDE4D2 CD mutant" also includes analogs of an engineered PDE4D2 CD or PDE4D2 CD polypeptide.
5 By "analog" is intended that a DNA or polypeptide sequence can contain alterations relative to the sequences disclosed herein, yet retain all or some or an enhanced degree of the biological activity of those sequences.
Anaaogs can be derived from genomic nucleotide sequences or from other organisms, or can be created synthetically. Those of skill in the art will appreciate that other analogs, as yet undisclosed or undiscovered, can be used to design and/or construct PDE4D2 CD or PDE4D2 CD mutant analogs. There is no need for a PDE4D2, CD or PDE4D2 CD mutant polypeptide to comprise all or substantially all of the amino acid sequence of SEQ ID NOs:2 or 4. Shorter or longer sequences can be employed in the 15 presently disclosed subject matter; shorter sequences are herein referred to as "segments". Thus, the terms "engineered PDE4.D2 CD" and "PDE4D2 CD mutant" also include fusion, chimeric or recombinant PDE4D2 CD, or PDE4D2 CD mutant polypeptides and proteins comprising sequences of the presently disclosed subject matter. Methods of preparing such proteins are 2o disclosed herein above and are known in the art.
IX.A.1. Sequences That Are Substantially Identical to a PDE4D2 or PDE4D2 CD Mutant Seauence of the Presently disclosed subject matter Nucleic acids that are substantially identical to a nucleic acid 2s sequence of a PDE4D2 or PDE4D2 CD mutant of the presently disclosed subject matter, i.e. allelic variants, genetically altered versions of the gene, etc., bind to a PDE4D2 or PDE4D2CD mutant sequence under stringent hybridization conditions. By using probes, particularly labeled probes of DNA sequences, one can isolate homologous or related genes. The source 30 of homologous genes can be any organism, including, but not limited to primates; rodents, such as rats and mice; canines; felines; bovines; equines;
yeast; and nematodes.

Among mammalian species, i.e. human and mouse, homologs can have substantial sequence similarity, i.e. at least 75% sequence identity between nucleotide sequences. Sequence similarity is calculated based on a reference sequence, which can be a subset of a larger sequence, such as s a conserved motif, coding region, flanking region, etc. in one embodiment, a reference sequence is at least about 18 nucleofiides (nt) long, in another embodiment at least about 30 nt long, and can extend to the complete sequence that is being compared. Algorithms for sequence analysis are known in the art, such as BLAST, described in Altschul et aL, J Mol Biol 215:403-10, 1990.
Percent identity or percent similarity of a DNA or peptide sequence can be determined, for example, by comparing sequence information using the GAP computer program, available from the University of Wisconsin Genetics Computer Group (now part of Accelrys Inc, San Diego, California, ~5 United States of America). The GAP program utilizes the alignment method of Needleman et ai., J Mol Biol, 48:443, 1970, as revised by Smith et al., Adv Appl Math, 2:482-89, 1981. Briefly, the GAP program defines similarity as the number of aligned symbols (i.e., nucleotides or amino acids) that are similar, divided by the total number of symbols in the shorter of the two 2o sequences. Exemplary parameters for the GAP program are the default parameters, which do not impose a penalty for end gaps. See i.e., Schwartz et ai., eds., Atlas of Protein Seguence and Structure. National Biomedical Research Foundation, pp. 357-358, 1979, and Gribskov et ai., Nucl Acids Res, 14: 6745-63, 1986.
25 The term "similarity" is contrasted with the term "identity". Similarity is defined as above; "identity", however, refers to a nucleic acid or amino acid sequence having the same amino acid at the same relative position in a given family member of a gene family. Homology and similarity are generally viewed as broader terms than the term identity. Biochemically 3o similar amino acids, for example leucine/isoleucine or glutamate/aspartate, can be present at the same position - these are not identical per se, but are biochemically "similar." As disclosed herein, these are referred to as conservative differences or conservative substitutions. This difFers from a conservative mutation at the DNA level, which changes the nucleotide sequence without making a change in the encoded amino acid, i.e. TCC to TCA, both of which encode serine.
As used herein, DNA analog sequences are "substantially identical" to s specific DNA sequences disclosed herein if: (a) the DNA analog sequence is derived from coding regions of the nucleic acid sequence shown in SEQ
ID NOs: 1 or 3; or (b) the DNA analog sequence is capable of hybridization with DNA sequences of (a) under stringent conditions and which encode a biologically active PDE4D2 or PDE4D2 CD gene product; or (c) the DNA
~o sequences are degenerate as a result of alternative genetic code to the DNA
analog sequences defined in (a) and/or (b). Substantially identical analog proteins and nucleic acids will have in one embodiment between about 70%
and 80%, in another embodiment between about 81 % to about 90%; and in still another embodiment between about 91 % and 99% sequence identity ~s with the corresponding sequence of the native protein or nucleic acid.
Sequences having lesser degrees of identity but comparable biological activity are considered to be equivalents.
As used herein, "stringent conditions" refers to conditions of high stringency, for example 6X SSC, 0.2% polyvinylpyrrolidone, 0.2% Ficoll, 20 0.2% bovine serum albumin, 0.1% sodium dodecyl sulfate, 100 pg/ml salmon sperm DNA, and 15% formamide at 68°C. For the purposes of specifying additional conditions of high stringency, preferred conditions comprise a salt concentration of about 200 mM and temperature of about 45°C. One example of stringent conditions is hybridization in 4X SSC, at 2s 65°C, followed by a washing in 0.1X SSC at 65°C for one hour.
Another exemplary stringent hybridization scheme uses 50% formamide, 4X SSC at 42°C.
In contrast, nucleic acids having sequence similarity are detected by hybridization under lower stringency conditions. Thus, sequence identity can 3o be determined by hybridization under lower stringency conditions, for example, at 50°C or higher and 0.1X SSC (9 mM NaCI/0.9 mM sodium citrate) and the sequences will remain bound when subjected to washing at 55°C in 1 X SSC.

IX.A.2. Complementarity and Hybridization to an Engineered PDE4D2 or PDE4D2 CD Mutant Sequence As used herein, the term "functionally equivalent codon" is used to refer to codons that encode the same amino acid, such as the ACG and AGU codons for serine. PDE4D2 or PDE4D2 CD-encoding nucleic acid sequences comprising SEO ID NOs:1 and 3, which have functionally equivalent codons are covered by the presently disclosed subject matter.
Thus, when referring to the sequence examples presented in SEQ ID NOs:1 and 3, applicants contemplate substitution of functionally equivalent codons into the sequence example of SEQ ID NOs:1 and 3. Thus, applicants are in possession of amino acid and nucleic acids sequences which include such substitutions but which are not set forth herein in their entirety for convenience.
It will also be understood by those of skill in the art that amino acid ~5 and nucleic acid sequences can include additional residues, such as additional N- or C-terminal amino acids or 5' or 3' nucleic acid sequences, and yet still be essentially as set forth in one of the sequences disclosed herein, so long as the sequence retains biological protein activity where polypeptide expression is concerned. The addition of terminal sequences 2o particularly applies to nucleic acid sequences which can, for example, include various non-coding sequences flanking either of the 5' or 3' portions of the coding region or can include various internal sequences, i.e., introns, which are known to occur within genes.
IX.B. Biologcal Eguivalents 25 The presently disclosed subject matter envisions and includes biological equivalents of PDE4D2 or PDE4D2 CD mutant polypeptide of the presently disclosed subject matter. The term "biological equivalent" refers to proteins having amino acid sequences which are substantially identical to the amino acid sequence of a PDE4D2 CD mutant of the presently disclosed 3o subject matter and which are capable of exerting a biological effect in that they are capable of binding a small molecule, binding a co-regulator, homo-or heterodimerizing or cross-reacting with anti-PDE4D2 or PDE4D2 CD

mutant antibodies raised against a mutant PDE4D2 or PDE4D2 CD
polypeptide of the presently disclosed subject matter.
For example, certain amino acids can be substituted for other amino acids in a protein structure without appreciable loss of interactive capacity s with, for example, structures in the nucleus of a cell. Since it is the interactive capacity and nature of a protein that defines that protein's biological functional activity, certain amino acid sequence substitutions can be made in a protein sequence (or the nucleic acid sequence encoding it) to obtain a protein with the same, enhanced, or antagonistic properties. Such properties can be achieved by interaction with the normal targets of the protein, but this need not be the case, and the biological activity of the presently disclosed subject matter is not limited to a particular mechanism of action. It is thus in accordance with the presently disclosed subject matter that various changes can be made in the amino acid sequence of a PDE4D2 ~5 or PDE4D2 CD mutant polypeptide of the presently disclosed subject matter or its underlying nucleic acid sequence without appreciable loss of biological utility or activity.
Biologically equivalent polypeptides, as used herein, are polypeptides in which certain, but not most or all, of the amino acids can be substituted.
2o Thus, when referring to the sequence examples presented in SEQ ID NOs:2 and 4, applicants envision substitution of codons that encode biologically equivalent amino acids, as described herein, into the sequence example of SEQ ID NOs:2 and 4, respectively. Thus, applicants are in possession of amino acid and nucleic acids sequences which include such substitutions 2s but which are not set forth herein in their entirety for convenience.
Alternatively, functionally equivalent proteins or peptides can be created via the application of recombinant DNA technology, in which changes in the protein structure can be engineered, based on considerations of the properties of the amino acids being exchanged, i. e. substitution of Ile 3o for Leu. Changes designed by man can be introduced through the application of site-directed mutagenesis techniques, i.e., to introduce improvements to the antigenicity of the protein or to test a PDE4D2 or PDE4D2 CD mutant polypeptide of the presently disclosed subject matter in order to modulate co-regulator-binding or ofiher activity, at the molecular level.
Amino acid substitutions, such as those which might be employed in modifying a PDE4D2 or PDE4D2 CD mutant polypeptide of the presently s disclosed subject matter are generally, but not necessarily, based on the relative similarity of the amino acid side-chain substituents, for example, their hydrophobicity, hydrophilicity, charge, size, and the like. An analysis of the size, shape and type of the amino acid side-chain substituents reveals that arginine, lysine and histidine are all positively charged residues; that alanine, glycine and serine are all of similar size; and that phenylalanine, tryptophan and tyrosine all have a generally similar shape. Therefore, based upon these considerations, arginine, lysine and histidine; alanine, glycine and serine; and phenylalanine, tryptophan and tyrosine; are defined herein as biologically functional equivalents. Those of skill in the art will appreciate ~s other biologically functional equivalent changes. It is implicit in the above discussion, however, that one of skill in the art can appreciate that a radical, rather than a conservative substitution is warranted in a given situation.
Non-conservative substitutions in mutant PDE4D2 or PDE4D2 CD
polypeptides of the presently disclosed subject matter are also an aspect of 2o the presently disclosed subject matter.
In making biologically functional equivalent amino acid substitutions, the hydropathic index of amino acids can be considered. Each amino acid has been assigned a hydropathic index on the basis of their hydrophobicity and charge characteristics, these are: isoleucine (+ 4.5); valine (+ 4.2);
2s leucine (+ 3.8); phenyfalanine (+ 2.8); cysteine (+ 2.5); methionine (+
1.9);
alanine (+ 1.8); glycine (-0.4); threonine (-0.7); serine (-0.8); tryptophan (-0.9); tyrosine (-1.3); proline (-1.6); histidine (-3.2); glutamate (-3.5);
glutamine (-3.5); aspartate (-3.5); asparagine (-3.5); lysine (-3.9); and arginine (-4.5).
3o The importance of the hydropathic amino acid index in conferring interactive biological function on a protein is generally understood in the art (Kyle & Doolittle, J Mol Biol, 157:105-132, 1982, incorporated herein by reference). It is known that certain amino acids can be substituted for other amino acids having a similar hydropathic index or score and still retain a similar biological activity. In one embodiment, amino acids for which the hydropathic indices are within ~2 of the original value are chosen, in another embodiment those within ~1 of the original value are chosen, and in still s another embodiment those within ~0.5 of the original value are chosen, in making amino acid changes based upon the hydropathic index.
It is also understood in the art that the substitution of like amino acids can be made effectively on the basis of hydrophilicity. U.S. Patent No.
4,554,101, incorporated herein by reference, states that the greatest local ~o average hydrophilicity of a protein, as governed by the hydrophilicity of its adjacent amino acids, correlates with its immunogenicity and antigenicity, i.e.
with a biological property of the protein. It is understood that an amino acid can be substituted for another having a similar hydrophilicity value and still obtain a biologically equivalent protein.
15 As detailed in U.S. Patent No. 4,554,101 to Hopa, the following hydrophilicity values have been assigned to amino acid residues: arginine (+
3.0); lysine (+ 3.0); aspartate (+ 3.0~1 ); glutamate (+ 3.0~1 ); serine (+
0.3);
asparagine (+ 0.2); glutamine (+ 0.2); glycine (0); threonine (-0.4); proline (-0.5~1 ); alanine (-0.5); histidine (-0.5); cysteine (-1.0); methionine (-1.3);
2o valine (-1.5); leucine (-1.8); isoleucine (-1.8); tyrosine (-2.3);
phenylalanine (-2.5); tryptophan (-3.4).
In making changes based upon similar hydrophilicity values, in one embodiment amino acids whose hydrophilicity values are within ~2 of the original value are chosen, in another embodiment those that are within -~1 of 2s the original value are chosen, and in still another embodiment those within ~0:5 of the original value are chosen, in making changes based upon similar hydrophilicity values.
While discussion has focused on functionally equivalent polypeptides arising from amino acid changes, it will be appreciated that these changes so can be effected by alteration of the encoding DNA, taking into consideration also that the genetic code is degenerate and that two or more codons can code for the same amino acid.
119' Thus, it will also be understood that presently disclosed subject matter is not limited to the particular nucleic acid and amino acid sequences of SEQ
ID NOs:1-4. Recombinant vectors and isolated DNA segments can therefore variously include a PDE4D2 or PDE4D2 CD mutant polypeptide-encoding region itself, include coding regions bearing selected alterations or modifications in the basic coding region, or include larger polypeptides which nevertheless comprise a PDE4D2 or PDE4D2 CD mutant polypeptide-encoding regions or can encode biologically functional equivalent proteins or polypeptides which have variant amino acid sequences. Biological activity of ~o a PDE4D2 or PDE4D2 CD mutant polypeptide can be determined, for example, by employing binding assays known to those of skill in the art.
The nucleic acid segments of the presently disclosed subject matter, regardless of the length of the coding sequence itself, can be combined with other DNA sequences, such as promoters, enhancers, polyadenylation signals, additional restriction enzyme sites, multiple cloning sites, other coding segments, polyhistidine encoding segments and the like, such that their overall length can vary considerably. It is therefore contemplated that a nucleic acid fragment of almost any length can be employed, with the total length preferably being limited by the ease of preparation and use in the 2o intended recombinant DNA protocol. For example, nucleic acid fragments can be prepared which include a short stretch complementary to a nucleic acid sequence set forth in SEQ ID NOs:1 and 3, such as about f0 nucleotides, and which are up to 10,000 or 5,000 base pairs in length. DNA
segments with total lengths of about 4,000, 3,000, 2,000, 1,000, 500, 200, 2s 100, and about 50 base pairs in length are also useful.
The DNA segments of the presently disclosed subject matter encompass biologically functional equivalents of PDE4D2 or PDE4D2 CD
mutant polypeptides. Such sequences can arise as a consequence of codon redundancy and functional equivalency that are known to occur naturally so within nucleic acid sequences and the proteins thus encoded. Alternatively, functionally equivalent proteins or polypeptides can be created via the application of recombinant DNA technology, in which changes in the protein structure can be engineered, based on considerations of the properties of the amino acids being exchanged. Changes can be introduced through the application of site-directed mutagenesis techniques, i.e., to introduce improvements to the antigenicity of the protein or to test variants of a PDE4D2 or PDE4D2 CD mutant of the presently disclosed subject matter in order to examine the degree of lipid-binding activity, or other activity at the molecular level. Various site-directed mutagenesis techniques are known to those of skill in the art and can be employed in the presently disclosed subject matter.
The presently disclosed subject matter further encompasses fusion proteins and peptides wherein a PDE4D2 or PDE4D2 CD mutant coding region of the presently disclosed subject matter is aligned within the same expression unit with other proteins or peptides having desired functions, such as for purification or immunodetection purposes.
Recombinant vectors form important further aspects of the presently ~5 disclosed subject matter. Particularly useful vectors are those in which the coding portion of the DNA segment is positioned under the control of a promoter. The promoter can be that naturally associated with a PDE4D2 gene, as can be obtained by isolating the 5' non-coding sequences located upstream of the coding segment or exon, for example, using recombinant 2o cloning andlor polymerise chain reaction (PCR) technology andlor other methods known in the art, in conjunction with the compositions disclosed herein.
In other embodiments, certain advantages can be gained by positioning the coding DNA segment under the control of a recombinant, or 25 heterologous, promoter. As used herein, a recombinant or heterologous promoter is a promoter that is not normally associated with a PDE4D2 gene in its natural environment. Such promoters can include promoters isolated from bacterial, viral, eukaryotic, or mammalian cells. Naturally, it will be important to employ a promoter that effectively directs the expression of the 3o DNA segment in the cell type chosen for expression. The use of promoter and cell type combinations for protein expression is generally known to those of skill in the art of molecular biology (see e.g., Sambrook et al., (1989) Molecular Cloningi: A Laboratory Manual, Cold Spring Harbor Laboratory (2"d ed.), New York, specifically incorporated herein by reference). The promoters employed can be constitutive or inducible and can be used under the appropriate conditions to direct high level expression of the introduced DNA segment, such as is advantageous in the large-scale production of s recombinant proteins or peptides. One representative promoter system contemplated for use in high-level expression is a T7 promoter-based system .
X. The Role of the Three-Dimensional Structure of the PDE4D2 LDB in Solving Additional PDE4D2 Crystals Because polypeptides can crystallize in more than one crystal form, the structural coordinates of a PDE4D2 CD, or portions thereof, in complex with a co-regulator as provided by the presently disclosed subject matter, are particularly useful in solving the structure of other crystal forms of PDE4D2 and the crystalline forms of other PDEs. The coordinates provided in the 15 presently disclosed subject matter can also be used to solve the structure of PDE4D2 or PDE4D2 CD mutants (such as those above), PDE4D2 LDB co-compfexes, or the crystalline form of any other protein with significant amino acid sequence homology to any functional domain of PDE4D2.
One method that can be employed for the purpose of solving 2o additional PDE4D2 crystal structures is molecular replacement. See generally, Rossmann, ed., The Molecular Replacement Method, Gordon &
Breach, New York, 1972. In the molecular replacement method, an unknown crystal form, whether it is another crystal form of a PDE4D2 or a PDE4D2 CD, (i.e. a PDE4D2 or a PDE4D2 CD mutant), a PDE4D2 or a 2s PDE4D2 CD polypeptide in complex with another compound (i.e. a "co-complex") or the crystal of some other protein with significant amino acid sequence homology to any functional region of the PDE4D2 CD (i.e. another PDE), can be determined using the PDE4D2 CD structure coordinates provided in Tables 4-5. This method provides an accurate structural form for so the unknown crystal more quickly and efficiently than attempting to determine such information ab initio.
In addition, in accordance with presently disclosed subject matter, PDE4D2 'or PDE4D2 CD mutants can be crystallized in complex with known modulators, such as a co-regulator. The crystal structures of a series of such complexes can then be solved by molecular replacement and compared with that of wild-type PDE4D2 or the wild-type PDE4D2, CD.
Potential sites for modification within the various binding sites of the enzyme s can thus be conveniently identified. This information provides an additional tool for identifying efficient binding interactions, for example, increased hydrophobic interactions between the PDE4D2 CD and a chemical entity or compound.
All of the complexes referred to in the present disclosure can be ~o studied using X-ray diffraction techniques (See i.e., Blundell & Johnson, Meth Enzymol, 114A & 1158, Wyckoff et al., eds., Academic Press, 1985) and can be refined using computer software, such as the X-PLORT"~
program (Brunger, X-PLOR, Version 3.1. A System for X-ray CrystalloqraphY and NMR, Yale University Press, New Haven, Connecticut, ~5 United States of America, 1992b; X-PLOR is available from Accelrys Inc, San Diego, California, United States of America}. This information can thus be used to optimize known classes of PDE4D2 and PDE4D2 CD ligands, and more importantly, to design and synthesize novel classes of PDE4D2 and PDE4D2 CD ligands, including co-regulators.
2o Examples The following Examples have been included to illustrate exemplary modes of the presently disclosed subject matter. Certain aspects of the following Examples are described in terms of techniques and procedures found or contemplated by the present inventors to work well in the practice of 2s the presently disclosed subject matter. These Examples are exemplified through the use of standard laboratory practices of the inventors. In light of the present disclosure and the general level of skill in the art, those of skill will appreciate that the following Examples are intended to be exemplary only and that numerous changes, modifications, and alterations can be 3o employed without departing from the spirit and scope of the presently disclosed subject matter.
Example 1 Protein Expression and Purification The EST (expressed sequence tag) cDNA clone of PDE4D2 (BF059733) was purchased from the American Type Culture Collection (ATCC). The protein expression and purification of the catalytic domain of PDE4D2 (amino acids 79-438) was described previously (Huai et al., 2003). Briefly, s the EST cDNA clones of PDE4D2 (BF059733) were purchased from ATCC
and subcloned following standard methods. The coding regions' for amino acids 79-438 of PDE4D2 were amplified by PCR and subcloned into the expression vector pET15b. The resulting plasmid pET-PDE4D2 was transformed into E. coli strain BL21-CODONPLUS~ (Stratagene, Inc., La ~o Jolla, California, United States of America) for overexpression. The E.
coli cell carrying pET-PDE4D2 was grown in LB medium at 37°C to absorption ODsoo = 0.7 and then 0.1 mM isopropyl ~3-D-thiogalactopyranoside was added for further growth at 12°C for 40 hours. The recombinant PDE4D2 was purified by Ni-NTA affinity column (Qiagen Inc., Valencia, California, ~s United States of America), thrombin cleavage, Q-SEPHAROSE"'" (available from Amersham Biosciences Corp., Piscataway, New Jersey, United States of America) and SUPERDEX 200T"" (available from Amersham Biosciences Corp., Piscataway, New Jersey, United States of America) columns. The PDE4D2 protein had a purity of greater than 95% as shown in by SDS-2o PAGE and was apparently a dimer as judged on the basis of the molecular sieving column. A typical purification yielded over 100 mg PDE4D2 from a 2 liter cell culture.
Example 2 Cr~tallization and Data Collection 25 The crystals were grown by vapor diffusion against a well buffer of 50 mM HEPES (pH 7.5), 15% PEG3350, 25% ethylene glycol, 5% methanol, and 5% DMSO at 4°C. The protein drop was prepared by mixing 10 mM
CAMP and 0.4 mM zinc sulfate with 15 mg/mL PDE4D2 in a storage buffer of 50 mM NaCI, 20 mM Tris-HCI (pH 7.5), and 1 mM f3-mercaptoethanol for the so crystallization. To saturate the CAMP binding, the crystals were soaked in a buffer of 50 mM HEPES (pH 7.5), 20% PEG3350, 25% ethylene glycol, 0.4 mM zinc sulfate, and 50 mM cAMP at room temperature for 5 hours and then immediately dipped into liquid nitrogen. The crystals of PDE4D2 have the space group P2~2~2~ with cell dimensions of a = 99.2 k, b = 111.2 A, and c =
159.7 A. The diffraction data were collected on beamline 14C of APS at Argonne National Labaratory (Table 3) and processed by program HKL
(Otwinowski and Minor, 1997).
s Examale 3 Structure Determination and Refinement The structure of PDE4D2 in complex with AMP was solved by the direct application of the tetramer of the PDE4D2-roliprarn structure to the crystal system (Huai et al., 2003). The orientation of the individual subunits in the PDE4D2-AMP tetramer was optimized by rigid-body refinement of CNS (Brianger, 1998). The electron density map was improved by the density modification package of CCP4 (1994). The atomic model was rebuilt by program O (Jones et al., 1991 ) and refined by CNS. See Table 3 for a summary of the statistics of the structure.
~5 Table 1 Interfacial Interactions in PDE4D2-AMP
Hydrogen bond Betweenchains A or B and D
and C

Arg116 NE ... GIu349 OE2 2.77 3.45 3.37 3.00 Arg116 NH2 GIu349 OE1 2.74 3.33 2.43 2.65 ... GIu349 OE2 3.15 3.52 2.90 3.06 ...

Asp151 OD1 Arg346 NH1 2.63 3.10 2.78 3.21 ... Arg350 NH2 2.90 3.37 3.13 2.70 ...

Thr215 O ... GIu244 N 2.82 2.80 2.94 2.80 Asn216 ND2 GIu244 OE1 2.98 2.63 2.87 3.04 ...

Arg350 NH1 Thr148 OG1 3.00 3.38 2.78 3.50 ...

Arg350 NH2 Thr148 OG1 3.20 2.90 3.35 3.64 ...

Betweenchains A
and B or C and D

Asn214 O ... Lys254 NZ 2.78 4.05 2.84 6.78 Asn214 OD1 GIn258 NE2 4.60 2.80 2.96 5.98 ...

Asn216 OD1 Lys254 NZ 2.76 3.24 2.97 2.97 ...

Tyr223 OH ... Met222 O 2.79 3.45 3.56 2.83 Asn224 ND2 ... Asn231 OD1 2.90 2.92 3.05 2.73 ... Asn231 O 3.00 3.46 3.97 3.05 Asp225 OD1 ... Arg261 NH2 3.23 3.34 2.93 4.95 Asp225 OD2 ... Arg261 NE 2.61 2.68 2.99 3.09 ... Arg261 NH2 3.26 3.46 3.37 3.44 Between chains A and D or B and C

GIu244 OE1 ... Lys254 NZ 3.03 2.75 2.96 2.63 GIu244 OE1 ... Arg257 NH1 2.96 2.97 6.40 4.99 GIu244 OE2 ... Arg257 NH2 2.78 2.82 7.60 5.68 Van der Waals interactions Between chains A and C or B and D

Asn214 ... GIu244 Thr215 ... GIu244, GIu243 Asn216 ... GIu243, GIu244, Lys254 Gfu218 ... Lys239 AIa220 ... Arg261 Arg346 ... Asp151 GIu349 ... Arg116, Met147 Arg350 ... Thr148, Asp151 Between chains A and B or C and D

Leu221 ... Arg261 Met222 ... Tyr223 Asn224 ... Arg261, I1e265, Asn231, Leu234 Asp225 ... Arg261 A1a235 ... Asn224 GIn242 ... Leu221 Lys254 ... Asn214, Asn216 GIn258 ... Asn214 Between chains A and D or B and C

Lys239 ... GIn242 GIu244 ... Lys254, Arg257 Table 2 AMP Interactions with the Active Site Residues of PDE4D2 AMP atoms PDE4D atoms Distance (A) O' His160 NE2 3.21,3.18,2.37,2.78 water W5 2.51,2.88,3.66 OL His160 NE2 2.50,3.06,3.18,2.80 Zn2 3.02, 2.75,2.38, 3.04 water W3 2.75,3.33,2.67,2.61 OR Asp2010D2 3.01,3.27,2.72,2.73 Asp318 OD2 2.85,2.66,2.91,3.03 Zn2 2.41, 2.46, 3.13, 2.45 Zn1 2.32,2.38,2.17,2.29 Water W4 3.33,3.27,3.30,3.82 N1 GIn369 NE2 2.86,3.26,3.05,3.22 N6 Asn3210D1 2.82,2.76,2.88,2.90 N7 ~ Asn321 ND2 3.31,3.35,3.13,2.97 Van der Waals contacts Phosphate Tyr 159, His160, His164, His200, Asp201, Asp318 Ribose His160, Met273, Asp318, Leu319, 11e336, Phe340, Phe372 Base Tyr159, Leu319, Asn321, Thr333, I1e336, GIn369, Phe372 Table 3 Statistics on Diffraction Data and Structure Refinement Data collecfion PDE4D2-AMP unligated PDE4D2 Space group P2~2~2~ P2~2~2~

Unit cell (a, b, 99.2,111.2,159.7 99.3,112.5,159.6 c, A) Resolution (A) 2.3 2.0 Total measurements436,461 500,736 Unique reflections70,994 92,048 Completeness (%) 89.7 (72.6)* 76.0(6.6%) Average fib 20.5 (3.9) 13.4(1.4) Rmerge 0.079 (0.54) 0.091 (0.97) Structure Refinement R-factor 0.229 0.234 R-free 0.274 0.268 Resolution 50-2.3 A 50-2.0 Reflections 67,124 86, 019 RMS deviation for Bond 0.0066 A 0.006 Angle 1.18 1.12 Average B-factor (A2) All atoms 50.3 Protein 50.4 AM P 56.2 Zn1 42.0 Zn2 65.9 Water 34. 0 *The numbers in parentheses are for the highest resolution shell.

Table 4 Atomic Structure Coordinate Data Obtained from X-Ray Diffraction from the 5 Catalytic Domain of PDE4D2 in Complex with AMP
ATOM 1 CB ILEA 79 2.762 24.771 38.4561.00 100.00A C

ATOM 2 CG2 ILEA 79 4.169 24.793 37.8741.00 100.00A C

ATOM 3 CG1 ILEA 79 2.800 24.428 39.9511.00 100.00A C

ATOM 4 CD1 ILEA 79 1.432 24.192 40.5761.00 100.00A C

ATOM 5 C ILEA 79 2.772 27.244 39.0481.00 100.00A C

ATOM 6 O ILEA 79 2.577 27.338 40.2661.00 100.00A O

ATOM 7 N ILEA 79 1.975 26.465 36.7671.00 99.98 A N

ATOM 8 CA ILEA 79 2.060 26.151 38.2261.00 100.00A C

ATOM 9 N PROA 80 3.604 28.087 38.4011.00 100.00A N

ATOM 10 CD PROA 80 4.176 27.989 37.0401.00 100.00A C

ATOM 11 CA PROA 80 4.286 29.132 39.1761.00 100.00A C

ATOM 12 CB PROA 80 5.543 29.398 38.3481.00 100.00A C

ATOM 13 CG PROA 80 5.045 29.233 36.9461.00 99.98 A C

ATOM 14 C PROA 80 3.455 30.406 39.4041.00 100.00A C

ATOM 15 O PROA 80 2.911 30.982 38.4581.00 99.93 A O

ATOM 16 N ARGA 81 3.361 30.836 40.6601.00 100.00A N

ATOM 17 CA ARGA 81 2.612 32.046 40.9931.00 100.00A C

ATOM 18 CB ARGA 81 2.284 32.077 42.4881.00 100.00A C

ATOM 19 CG ARGA 81 0.926 31.487 42.8211.00 100.00A C

ATOM 20 CD ARGA S1 -0.18732.334 42.2161.00 99.83 A C

ATOM 21 NE ARGA 81 -1.50931.762 42.4531.00 100.00A N

ATOM 22 CZ ARGA 81 -2.65032.360 42.1231.00 100.00A C

ATOM 23 NH1 ARGA 81 -2.63233.552 41.5391.00 100.00A N

ATOM 24 NH2 ARGA 81 -3.80931.766 42.3741.00 99.63 A N

ATOM 25 C ARGA 81 3.389 33.300 40.6041.00 100.00A C

ATOM 26 O ARGA 81 4.298 33.727 41.3211.00 100.00A O

ATOM 27 N PHEA 82 3.010 33.881 39.4651.00 _ A N
99.95 ATOM 28 CA PHEA 82 3.658 35.080 38.9231.00 100.00A C

ATOM 29 CB PHEA 82 3.829 36.161 40.0071.00 100.00A C

ATOM 30 CG PHEA 82 2.549 36.546 40.7031.00 100.00A C

ATOM 31 CD1 PHEA 82 1.394 36.821 39.9711.00 _ A C
100.0 ATOM 32 CD2 PHEA 82 2.508 36.662 42.0921.00 _ A C
100.0 ATOM 33 CE1 PHEA 82 0,216 37.205 _ 40.6151.00 _ A C
~ ~ 100.00 ATOM 34 CE2 PHEA 82 1.338 37.046 42.7481.00 100.00A C

ATOM 35 CZ PHEA 82 0.188 37.317 42.0101.00 100.00A C

ATOM 36 C PHEA 82 5.031 34.732 38.3341.00 99.83 A C

ATOM 37 O PHEA 82 6.039 35.363 38.6641.00 100.00A O

ATOM 38 N GLYA 83 5.069 33.730 37.4591.00 99.12 A N

ATOM 39 CA GLYA 83 6.322 33.328 36_8441.00 97.85 A C

ATOM 40 C GLYA 83 7.401 32.959 37.8501.00 96.94 A C

ATOM 41 O GLY~ 83 8.562 32.767 37.4821.00 97.01 A O
A

ATOM 42 N VAL~ 84 7.018 32.866 39.1221.00 _ A N
A 95.80 ATOM 43 CA VALA 84 7.954 32.514 40.1871.00 94.29 A C

ATOM 44 CB VALA 84 7.824 33.464 41.3891.00 94.78 A C

ATOM 45 CG1VALA 84 8.899 33.137 42.4141.00 95.11 A C
ATOM 46 CG2VALA 84 7.960 34.904 40.9291.00 94.97 A C

ATOM 47 C VALA 84 7.725 31.078 40.6641.00 92.66 A C

ATOM 48 O VALA 84 __6.61830.708 41.0631.00 92.26 A O

ATOM 49 N LYSi 85 8.795 30.288 40.6311.00 90.87 A N
A

ATOM 50 CA LYSA 85 8.780 28.877 41.0111.00 88.79 A C

ATOM 51 CB LYSA 85 10.21428.399 49.2631.00 88.92 A C

ATOM 52 CG LYSA 85 11.24228.924 40.2901.00 88.40 A C

ATOM 53 CD LYSA 85 12.64428.670 40.8241.00 88.69 A C

ATOM 54 CE LYSA 85 13.68729.495 40.0971.00 88.42 A C

ATOM 55 NZ LYSA 85 15.04429.273 40.6741.00 88.79 A N

ATOM 56 C LYSA 85 7.933 28.484 42.2171.00 86.95 A C

ATOM 57 O LYSA 85 7.580 29.310 43.0591.00 86.44 A O

ATOM 58 N THRA 86 7.523 27.192 42.2771.00 85.07 A N

ATOM 59 CA THRA 86 6.858 26.609 43.3691.00 83.27 A C

ATOM 60 CB THRA 86 6.002 25.427 42.8751.00 83.14 A C

ATOM 61 OG1THRA 86 5.257 25.827 41.7161.00 82.72 A O

ATOM 62 CG2THRA 86 5.038 24.973 43.9601.00 82.74 A C

ATOM 63 C THRA 86 7.950 26.091 44.2991.00 82.19 A C

ATOM 64 O THRA 86 9.100 25.972 43.8791.00 82.17 A O

ATOM 65 N GLUA 87 7.610 25.754 45.5431.00 80.76 A N

ATOM 66 CA GLUA 87 8.615 25.298 46.4851.00 79.40 A C

ATOM 67 CB GLUA 87 8.323 25.838 47.8841.00 80.46 A C

ATOM 68 CG GLUA 87 8.802 27.273 48.0881.00 81.13 A C

ATOM 69 CD GLUA 87 10.29427.356 48.3731.00 51.74 A C

ATOM 70 OE1GLUA 87 10.73026.785 49.3961.00 81.86 ' O
A

ATOM 71 OE2GLUA 87 11.02927.990 47.5821.00 82.51 A O

ATOM 72 C GLUA 87 8.761 23.779 46.5101.00 78.05 A C

ATOM 73 O GLUA 87 8.658 23.133 47.5531.00 78.04 A O

ATOM 74 N GLNA 88 9.004 23.233 45.3241.00 76.24 A N

ATOM 75 CA GLNA 88 9.206 21.809 45.0681.00 74.10 A C

ATOM 76 CB GLNA SS 7.878 21.052 45.0241.00 74.98 A C

ATOM 77 CG GLNA 88 8.032 19.617 44.5391.00 76.08 A C

ATOM 78 CD GLNA 88 6.708 18.952 44.2131.00 77.38 A C

ATOM 79 OE1GLNA 88 5.919 19.468 43.4151.00 78.01 A O

ATOM 80 NE2GLNA 88 6.462 17.794 44.8191.00 77.16 A N

ATOM 81 C GLNA 88 9,792 21.863 43.6691.00 71.96 A C

ATOM 82 O GLNA 88 10.76421.183 43.3401.00 70.97 A O

ATOM 83 N GLUA 89 9.162 22.706 42.5601.00 69.39 A N

ATOM 84 CA GLUA 89 9.576 22.966 41.4981.00 67.35 A C

ATOM 85 CB GLUA 89 8,518 23.850 40.8251.00 68.06 A C

ATOM 86 CG GLUA 89 8.868 24.397 39.4551.00 70.63 A C

ATOM 87 CD GLUA 89 7.693 25.139 38.8161.00 72.78 A C

ATOM 88 OE1GLUA 89 6.839 25.672 39.5671.00 72.45 A O

ATOM 89 OE2GLUA 89 7.633 25.200 37.5631.00 73.69 A O

ATOM 90 C GLUA 89 10.92623.683 41.6351.00 65.04 A C

ATOM 91 O GLUA 89 11.75423.663 40.7251.00 64.31 A O

ATOM 92 N ASPA 90 11.14224.293 42.7991.00 62.34 A N

ATOM 93 CA ASPA 90 12.39124.987 43.0971.00 60.36 A C

ATOM 94 CB ASPA 90 12.23025.884 44.3261.00 61.07 A C

ATOM 95 CG ASPA 90 13.54526.511 44.7691.00 61.81 A C

ATOM 96 ODtASPA 90 13.75726.639 45.9971.00 62.58 A O

ATOM 97 OD2ASPA 90 14.36126.881 43.8931.00 61.23 A 0 ATOM 98 C ASPA 90 13.47023.944 43.3851.00 58.46 A C

ATOM 99 O ASPA 90 14.59924.051 42.8991.00 58.07 A 0 ATOM 100 N VALA 91 13.10822.945 44.1881.00 55.85 A N

ATOM 101 CA VALA 91 14.01121.862 44.5581.00 53.67 A C

ATOM 102 CB VALA 91 13.34620.898 45.5541.00 54.98 A C
' ATOM 103 CG1VALA 91 14.26319.716 45.8321.00 _ A C
55.61 ATOM 104 CG2VALA 91 13.02821.634 4_6.8491.00 __ A C
_ 55.61 ATOM 105 C VALA 91 14.39221.079__ 43.3181.00 _ A C
~ 52.1 ~ 4 ATOM 106 O VALA 91 15.50720.575 43.2111.00 _ A O
50.41 ATOM 107 N LEUA 92 13.44720.980 42.3861.00 _ A N
J 51.29 ATOM 108 CA LEUA 92 13.66020.273 41.1291.00 49.50 A C

ATOM 109 CB LEUA 92 12.36520.246 40.3091.00 50.32 A C

ATOM 110 CG LEUA 92 12.18019.235 39.1721.00 49.68 A C

ATOM 111 CD1LEUA 92 10.98119.664 38.3561.00 50.91 A C

ATOM 112 CD2LEUA 92 _13_.40319.155 38.2861.00 50.29 A C

ATOM 113 C LEUA 92 14.71621.058 40.3671.00 48.72 A C

ATOM 114 0 LEUA 92 15.65020.490 39.8451.00 47.06 A O

ATOM 115 N ALAA 93 14.51822.374 40.3191.00 47.56 A N

ATOM 116 CA ALAA 93 15.42823.273 39.6251.00 46.92 A C

ATOM 117 CB ALAA 93 14.95724.713 39.7831.00 45.76 A C

ATOM 118 C ALAA 93 16.85823.133 40.1301.00 47.03 A C

ATOM 119 0 ALAA 93 17.80423.132 39.3381.00 46.97 A O

ATOM 120 N LYSA 94 17.01723.011 41.4451.00 46.51 A N

ATOM 121 CA LYSA 94 . 18.34822.884 42.0311.00 47.23 A C

ATOM 122 CB LYSA 94 18.29623.187 43.5261.00 47.07 A C

ATOM 123 CG LYSA 94 17.87924.610 43.7791.00 47.21 A C

ATOM 124 CD LYSA 94 17.96924.984 45.2181.00 47.90 A C

ATOM 125 CE LYSA 94 17.48326.400 45.3921.00 48.29 A C

ATOM 126 NZ LYSA 94 17.55526.775 46.8121.00 50.26 A N

ATOM 127 C LYSA 94 18.98221.525 41.7911.00 46.80 A C

ATOM 128 O LYSA 94 20.20721.391 41.8031.00 46.74 A O

ATOM 129 N GLUA 95 18.14820.512 41.5891.00 46.91 A N

ATOM 130 CA GLUA 95 18.65219.180 41.3051.00 47.00 A C

ATOM 131 CB GLUA 95 17.53618,149 41.4581.00 48.25 A C

ATOM 132 CG GLUA 95 17.31217.663 42.8781.00 50.79 A C

ATOM 133 CD GLUA 95 18.53416.981 43.4631.00 51.05 A C

ATOM 134 OE1GLUA 95 19.19016.208 42.7431.00 51.53 A 0 ATOM 135 OE2GLUA 95 18.84117.205 44.6501.00 54.33 A 0 ATOM 136 C GLUA 95 19.16219.195 39.8611.00 46.62 A C

ATOM 137 O GLUA 95 20.14018.516 39.5241.00 46.65 A O

ATOM 138 N LEUA 96 18.49719.998 39.0271.00 44.88 A N

ATOM 139 CA LEUA 96 18.53620.138 37.6181.00 44.15 A C

ATOM 140 CB LEUA 96 17.64220.688 36.$371.00 44.13 A C

ATOM 141 CG LEUA 96 16.50719.716 36.4911.00 45.32 A C

ATOM 142 CD1LEUA 96 15.29920.489 35.9621.00 44.84 A C

ATOM 143 CD2LEUA 96 16.99518.705 35.4621.00 44.66 A C

ATOM 144 C LEUA 96 20.04821.018 37.3661.00 44.86 A C

ATOM 145 O LEUA 96 20.28621.448 36.2401.00 45.39 A O

ATOM 146 N GLUA 97 20.81621.314 38.4021.00 45.42 A N

ATOM 147 CA GLUA 97 22.00922,120 38.1961.00 46.47 A C

ATOM 148 CB GLUA 97 22.26823.012 39.4121.00 48.53 A C

ATOM 149 CG GLUA 97 21.46624:317 39.3521.00 51.65 A C

ATOM 150 CD GLUA 97 21.65225.190 40.5681.00 52.47 A C

ATOM 151 OEtGLUA 97 22.75325.139 41,1571.00 53.74 A O

ATOM 152 OE2GLUA 97 20.70525.933 40.9231.00 53.02 A O

ATOM 153 C GLUA 97 23.17821.178 37.9261.00 46.32 A C

ATOM 154 O GLUA 97 24.27821.603 37.5701.00 45.96 A O

ATOM 155 N ASPA 98 22.90619.883 38.0721.00 45.78 A N

ATOM 156 CA ASPA 98 23,89618.842 37.8401.00 45.38 A C

ATOM 157 CB ASPA 98 23.84017.792 38.9551.00 46.39 A C

ATOM 158 CG ASPA 98 24.36818.307 40.2801.00 48.46 A C

ATOM 159 OD1ASPA 98 25.34119.098 40.2711.00 49.02 A O

ATOM 160 OD2ASPA 98 23.82317.903 41.3331.00 49.76 A O

ATOM 161 C ASPA 98 23.66218.146 36.4981.00 44.20 A C

ATOM 162 O ASPA 98 24.15717.038 36.2771.00 43.52 A O

ATOM 163 N VALA 99 22.91618.795 35.6061.00 42. A N

ATOM 164 CA VALA 99 22.60418.213 34.2991.00 _ A C
41.21 ATOM 165 CB VALA 99 21.75319.165 33.4311.00 40.83 A C

ATOM 166 CG1VALA 99 20.95118.376 32.4351.00 40.25 A C

ATOM 167 CG2VALA 99 20.84919.984 34.2831.00 41.10 A C

ATOM 168 C VALA 99 23.85917.881 33.5011.00 41.88 A C

ATOM 169 O VALA 99 23.89016.899 32.7561.00 41.47 A O

ATOM 17D N ASNA 10024.89218.702 33.6481.00 42.21 A N

ATOM 171 CA ASNA 10026.12518.476 32.9111 _ A C
.00 42.90 ATOM 172 CB ASNA 10026.85119.805 32.674_ 44.06 A C

.00 ATOM 173 CG ASNA 10025.94120.881 32.070_ 44.19 A C
1.00 ATOM 174 OD1ASNA 10025.33720.690 31.0161.00 43.31 A 0 ATOM 175 ND2ASNA 10025.84922.017 32.7451.00 43.90 A N

ATOM 176 C ASNA 10027.05517.503 33.6261.00 43.20 A C

ATOM 177 O ASNA 10028.20517.345 33.2291.00 43.65 A O

ATOM 178 N LYSA 10126.55216.836 34.6621.00 44.01 A N

ATOM 179 CA LYSA 10127.36415.887 35.4321.00 44.40 A C

ATOM 180 CB LYSA 10127.44016.330 36.8971.00 45.33 A C

ATOM 181 CG LYSA 10128.20517.633 37.1081.00 48.72 A C

ATOM 182 CD LYSA 10128.20818.067 38.56 1.00 49.92 A C

ATOM 183 CE LYSA 10128.88519.425 _ i.00 51.72 A C
38.7 ATOM 184 NZ LYSA 10128.77919.970 _ 1.00 52.99 A N
_ 40.114 ATOM 185 C LYSA 10126.92614.422 35.3891.00 44.51 A C

ATOM 186 O LYSA 10125.73314.093 35.4341.00 44.39 A 0 ATOM 187 N TRPA 10227.91813.545 35.3031.00 44.22 A N

ATOM 188 CA TRPA 10227.69312.109 35.2871.00 43.29 A C

ATOM 189 CB TRPA 10229.02611.390 3 1.00 43.78 A C

5.

ATOM 190 CG TRPA 10228.92210.026 _ 1.00 44.23 A C
_ 34.428 ATOM 191 CD2TRPA 10228.5269.722 33.0851.00 44.58 A C

ATOM 192 CE2TRPA 1022$.6378.321 32.9221.00 44.46 A C

ATOM 193 CE3TRPA 10228.09110.497 32.0001.00 45.32 A C

ATOM 194 CD1TRPA 10229.2408.832 35.0121.00 44.51 A C

ATOM 195 NE1TRPA 10229.0747.801 34.1121.00 44.94 A N

ATOM 196 CZ2TRPA 10228.3287.679 _ 1.00 43.89 A C
-31.718 ATOM 197 CZ3TRPA 10227.7819.854 30.7971.00 44.11 A C

ATOM 198 CH2TRPA 10227.9038.461 30.6701.00 44.12 A C

ATOM 199 C TRPA 10227.17511.800 36.6871.00 42.73 A C

ATOM 200 O TRPA 10227.74512.262 37.6681.00 44.32 A O

ATOM 201 N GLYA 10326.08311.056 36.7901.00 41.71 A N

ATOM 202 CA GLYA 10325,56510.730 38.1041.00 40.44 A C

ATOM 203 C GLYA 10324.42911.592 38.6201.00 39.71 A C
' ATOM 204 O GLYA 10324.20711.660 39.8271.00 39.98 A O

ATOM 205 N LEUA 10423.70912.256 37.7251.00 38.99 A N

ATOM 206 CA LEUA 10422.57313.083 38.1321.00 37.84 A C

ATOM 207 CB LEUA 10421.871 ~ 13.66036.8861.00 ~ 37.13A C

ATOM 208 CG LEUA 10420,599 14,49937.0621.00 36.93 A C

ATOM 209 CD1LEUA 10420.944 15.90837.5011.00 36.40 A C

ATOM 210 CD2LEUA 10419.840 14.54935.7401.00 38.35 A C

ATOM 211 C LEUA 10421.584 12.20538.9171.00 37.35 A C

ATOM 212 O LEUA 10421.405 11.03338.5971.00 36.03 A O

ATOM 213 N HISA 10520.957_12.77139.9451.00 38.92 A N

ATOM 214 CA HISA 10519.970 12.04940.7551.00 39.31 A C

ATOM 215 CB HISA 10519.639 12.83342.0311.00 41.45 A C

ATOM 216 CG HISA 10520.821 13.10442.9111.00 45.17 A C

ATOM 217 CD2HISA 10521.967 12.409__43.1101.00 46.32 A C

ATOM 218 ND1HISA 10520.898 14.21143.7331.00 46.74 A N

ATOM 219 CE7HISA 10522.040 14.18744.3961.00 47.15 A C

ATOM 220 NE2HISA 10522.708 _13.104_44.0361.00 47.74 A N

ATOM 221 C HISA 10518.721 11.98539.8911.00 39.51 A C

ATOM 222 O HISA 10517.730 12.66840.1661.00 40.79 A O

ATOM 223 N VALA 10618.759 11.16738.8491.00 38.22 A N

ATOM 224 CA VALA 10617.631 11.09637.9381.00 37.60 A C

ATOM 225 CB VALA 10617.987 10271 36.6671.00 37.70 A C

ATOM 226 CG1VALA 10618.323_8.841 37.D451.00 36.23 A C

ATOM 227 CG2VALA 10616.818 10.32135.6701.00 36.69 A C

ATOM 228 C VALA 10616.355 10.55538.5701.00 37.35 A C

ATOM 229 O VALA 10615.255 10.99738.2291.00 36.41 A O

ATOM 230 N PHEA 10716,499 9,603 39.4851.00 36.35 A N

ATOM 231 CA PHEA 10715.339 9,029 40.1471.00 36.27 A C

ATOM 232 CB PHEA 10715.749 7.804 40.9701.00 34.73 A C

ATOM 233 CG PHEA 10716,101 6.610 40.1301.00 35.50 A C

ATOM 234 CD1PHEA 10715.101 5.859 39.5131.00 34.52 A C

ATOM 235 CD2PHEA 10717.432 6.254 39.9271.00 33.78 A C

ATOM 236 CE1PHEA 10715,425 4.772 38.7081.00 35.78 A C
.

ATOM 237 CE2PHEA 10717.765 5.168 39.1221.00 33.65 A C

ATOM 238 CZ PHEA 10716.765 4.426 38.5111.00 35.70 A C

ATOM 239 C PHEA 10714.651 10.06741.0321.00 36.36 A C

ATOM 240 0 PHEA 10713.430 10.05841.1691.00 35.92 R O

ATOM 241' N ARGA 10815.425 10.96541.6271.00 36.79 A N

ATOM 242 CA ARGA 10814,810 11.97942.4611.00 38.50 A C

ATOM 243 CB ARGA 10815.846 12.74543.2971.00 41.37 A C

ATOM 244 CG ARGA 10815.143 13.59644.3521.00 47.52 A C

ATOM 245 CD ARGA 10816.057 14.31945.3231.00 52.82 A C

ATOM 246 NE ARGA 10815.248 15.12446.2451.00 57.13 A N

ATOM 247 CZ ARGA 10815.731 16.06047.0581.00 58.63 A C

ATOM 248 NH1ARGA 10817.035 16.32547.0781.00 58.92 A N

ATOM 249 NH2ARGA 10814.905 16.73847.8471.00 58.41 A N

ATOM 250 C ARGA 10814.064 12.94141.5421.00 38.00 A C

ATOM 251 O ARGA 10812.877 13.22441.7471.00 38.37 A O

ATOM 252 N ILEA 10914.764 13.42840.5211.00 36.04 A N

ATOM 253 CA ILEA 10914.171 14.33639.5511.00 33.98 A C

ATOM 254 CB ILEA 10915.148 14.59238.3761.00 34.23 A C

ATOM 255 CG2ILEA 10914.405 15.17337.1671.00 30.59 A C

ATOM 256 CG1ILEA 10916.271 15.51638.8631.00 33.03 A C

ATOM 257 CD1ILEA 10917.310 15.84237.5231.00 35.66 A C

ATOM 258 C ILEA 10912.860 13.74439.0391.00 32.77 A C

ATOM 259 O ILEA 10911.891 14.46838.7841.00 29.68 A O

ATOM 260 N ALAA 11012.824 12.42538.9061.00 32.50 A N

ATOM 261 CA ALAA 11011.602 11.77838.4471.00 35.33 A C

ATOM 262 CB ALAA 11011.838 10.29338.2141.00 34.28 A C

ATOM 263 C ALAA 11010.480 11.98739.4741.00 36.40 A C

ATOM 264 O ALAA 1109.350 12,32239.1111.00 36.27 A O

ATOM 265 N GLUA 11110.799 11.81740.7531.00 38.05 A N

ATOM 266 CA GLUA 1119.796 11.98641.8081.00 40.79 A C

ATOM 267 CB GLUA 11110.351 11.53343.1611.00 43.24 A C

ATOM 268 CG GLUA 11111.074 10.19443.1161.00 48.27 A C

ATOM 269 CD GLUA 11111.172 9.529 44.4801.00 51.43 A C

ATOM 270 OE1GLUA 11111.381 10.25046.4841.00 51.67 A O

ATOM 271 OE2GLUA 11111.048 8.280 44.5401.00 53.17 A 0 ATOM 272 C GLUA 1119,349 13.44041.9161.00 39.56 A C

ATOM 273 O GLUA 1118,157 13.73741.9721.00 38.35 A O

ATOM 274 N LEUA 11210.325 14.33641.9371.00 39.17 A N

ATOM 275 CA LEUA 11210.069 15.76542.0501.00 39.13 A C

ATOM 276 CS LEUA 11211.400 16.52142.1041.00 37.44 A C

ATOM 277 CG LEUA 11212.257 16.20643.3371.00 35.75 A C

ATOM 278 CD1LEUA 11213.608 16.95043.2941.00 32.47 A C

ATOM 279 CD2LEUA 11211.451 16.5974A.5651.00 33.51 A C

ATOM 280 C LEUA 1129.214 16.31940.9161.00 39.97 A C

ATOM 281 O LEUA 1128.296 17,11441.1471.00 40.42 A O

ATOM 282 N SERA 1139.502 15.88539.6941.00 ' 38.95A N

ATOM 283 CA SERA 1138.777 16.38038.5311.00 37.44 A C

ATOM 284 CB SERA 1139.632 16.20337.2741.00 36.63 A C

ATOM 285 OG SERA 1139.721 14.83636.9191.00 35,15 A O

ATOM 286 C SERA 1137.412 15.74238.3001.00 36.90 A C

ATOM 287 O SERA 1136.776 16.00237.2851.00 38.07 A O

ATOM 288 N GLYA 1146.953 14.91639.2301.00 36.93 A N

ATOM 289 CA GLYA 1145,668 14,26739.0491.00 35.78 A C

ATOM 290 C GLYA 1145.760 13.19137.9821.00 36.74 A C

ATOM 291 0 GLYA 1144.812 12.95637.2391.00 37.38 A O

ATOM 292 N ASNA 1156.913 12.53437.9081.00 36.70 A N

ATOM 293 CA ASNA 1157.154 11.47536.9311.00 37.28 A C

ATOM 294 CB ASNA 1156.048 10.413__ 1.00 37.05 A C
36.992 ATOM 295 CG ASNA 1156.433 9.135 36.2701.00 37.23 A C

ATOM 296 OD1ASNA 1157.602 8.747 36.2481.00 37.25 A O

ATOM 297 ND2ASNA 1155.449 8.465 35.6901.00 37.61 A N

ATOM 298 C ASNA 1157.261 12.05335.5241.00 36.53 A C

ATOM 299 O ASNA 1156.716 11.51634.5551.00 37.24 A 0 ATOM 300 N ARGA 1167.982 13.16235.4421.00 36.14 A N

ATOM 301 CA ARGA 1168.226 13.85734.1941.00 35.15 A C

ATOM 302 CB ARGA 1167.467 15.191__ 1.00 35.90 A C
34.186 ATOM 303 CG ARGA 1165.981 15.0_5933.8361.00 38.15 A C

ATOM 304 CD ARGA 1165.737 15.53032.4111.00 41.77 A C

ATOM 305 NE ARGA 1164.394 15.23631.9221.00 43.07 A N

ATOM 306 CZ ARGA 1164.017 14.05631:4371.00 44.26 A C

ATOM 307 NH1ARGA 1164.886 13.05431.3741.00 45.28 A N

ATOM 308 NH2ARGA 1162.775 13.87931.0101.00 43.19 A N

ATOM 309 C ARGA 1169.732 14.08834.0261.00 33.60 A C

ATOM 310 O ARGA 11610.163 15.16733.63 1.00 33.34 A O

ATOM 311 N PRO. 11710.557 13_.069_ 1.00 32.22 A N
A 34.333 ATOM 312 CD PRO; 11710.257 11.70034.7851.00 30.64 A C
A

ATOM 313 CA PROA 11712.006 13.25234.1811.00 31.55 A C

ATOM 314 CB PROA 11712.583 11.94334.7291.00 31.03 A C

ATOM 315 CG PROA 11711.519 10.94734.3831.00 30.24 A C

ATOM 316 C PROA 11712.418 13.48832.7281.00 30.44 A C

ATOM 317 O PROA 11713.352 14.24132.4641.00 29.26 A O

ATOM 318 N LEUA 11811.724 12.832_ 1.00 29.84 A N
31.796 ATOM 319 CA LEUA 11812.034 12.97530.3761.00 28.87 A C

ATOM 320 CB LEUA 11811.299 11.92529.5411.00 27.05 A C

ATOM 321 CG LEUA 11811.685 11.89628.0501,00 28.03 A C

ATOM 322 CD1LEUA 11813.173 11.57227.9211.00 24.84 A C

ATOM 323 CD2LEUA 11810.832 10.86527.2881.00 25.40 A C

ATOM 324 C LEUA 11811.670 14.36229.8721.00 28.49 A C

ATOM 325 O LEUA 11812.453 14.99829.1851.00 29.29 A O

ATOM 326 N THRA 11910.491 14.84830.2261.00 28.53 A N

ATOM 327 CA THRA 11910.095 16_17129.7731.00 29.50 A C

ATOM 328 CB THRA 1198.638 16.46130.1461.00 30.70 A C

ATOM 329 OG1THRA 1197.798 15.46529.5501.00 30.79 A O

ATOM 330 CG2THRA 1198.213 17.839_ 1.00 29.41 A C
29.655 ATOM 331 C THRA 11910.998 17.280_ 1.00 29.69 A C

.326 ATOM 332 O THRA 11911.496 18.116_ 1.00 30.38 A O
29.569 ATOM 333 N VALA 12011.250 17.27431.6281.00 28.61 A N

ATOM 334 CA VALA 12012.077 18.32732.2011.00 28.94 A C

ATOM 335 CB VALA 12011.932 18.39633.7361.00 30.30 A C

ATOM 336 CG1VALA 12010.475 _18.64634.0831.00 29.01 A C

ATOM 337 CG2VALA 12012.449 17.11034.3931.00 29.99 A C

ATOM 338 C VALA 12013.554 18.28331.8371.00 29.17 A C

ATOM 339 O VALA 12014.160 19.32731.5841.00 29.50 A O

ATOM 340 N ILEA 12114.152 17.10131.7901.00 28.51 A N

ATOM 341 CA ILEA 12115.564 17.05531.4301.00 28.55 A C

ATOM 342 CB ILEA 12116.183 15.67031.7311.00 28.60 A C

ATOM 343 CG2ILEA 12117.582 15.56631.1111.00 27.75 A C

ATOM 344 CG1ILEA 12116.249 15.47033.2561.00 25.46 A C

ATOM 345 CD1ILEA 12116.258 13.99833.7071.00 26.54 A C

ATOM 346 C ILEA 12115.775 17.43729.9571.00 27.81 A C

ATOM 347 O ILEA 12116.759 18.09229.fi271.00 26.25 A O

ATOM 348 N META 12214.854 17.03029.0801.00 27.86 A N

ATOM 349 CA META 12214.954 17.37927.6601.00 27.99 A C

ATOM 350 CB META 12213.885 16.65526.8421.00 27.67 A C

ATOM 351 CG META 12214.238 15.22926.4571.00 29.60 A C

ATOM 352 SD META 12215.475 15.10125.1271.00 28.65 A S

ATOM 353 CE META 12214.465 15.54423.7051.00 28.18 A C

ATOM 354 C META 12214.798 18.88727.4781.00 27.86 A C
.

ATOM 355 O META 12215.528 19.50326.7141.00 27.39 A O

ATOM 356 N HISA 12313.845 19.48028.1891.00 30.05 A N

ATOM 357 CA HISA 12313.617 20.92228.1081.00 32.37 A C

ATOM 358 CB HISA 12312.409 21.32128.9591.00 34.60 A C

ATOM 359 CG HISA 12312.151 22.79728.8941.00 37.68 A C

ATOM 360 CD2HISA 12312.325 23.70929.9811.00 38.65 A C

ATOM 361 ND1HISA 12311.647 23.49527.9161.00 38.24 A N

ATOM 362 CE1HISA 12311.519 24.77028.2371.00 38.37 A C

ATOM 363 NE2HISA 12311.924 24.92729.4841.00 39.59 A N

ATOM 364 C HISA 12314.854 21.67528.6051.00 33.13 A C

ATOM 365 O HISA 12315.278 22.66527.9971.00 34.12 A O

ATOM 366 N THRA 12415.419 21.20029.7141.00 32.15 A N

ATOM 367 CA THRA 12416.610 21.80130.3171.00 32.54 A C

ATOM 368 CB THRA 12417.036 21.01631.5891.00 33.94 A C

ATOM 369 OG1THRA 12415.956 21.00432.5271.00 36.08 A O

ATOM 370 CG2THRA 12418.274 21.64432.2441.00 33.48 A C

ATOM 371 C THRA 12417.775 21.78529.3231.00 31.13 A C

ATOM 372 O THRA 12418.471 22.784_ 1.00 31.02 A O
29.134 ATOM 373 N ILEA 12517.976 20.63528.6911.00 30.24 A N

ATOM 374 CA ILEA 12519.047 20.46627.7221.00 30.12 A C

ATOM 375 CB ILEA 12519.246 18.98627.3931.00 30.04 A C

ATOM 376 CG2ILEA 12520.186 18.83926.2101.00 28.65 A C

ATOM 377 CG1ILEA 12519.814 18.27328.6331.00 31.31 A C

ATOM 378 CD1ILEA 12520.017 16.78628.4671.00 32.27 A C

ATOM 379 C ILE A 12518.845 21.25426.43fi1.00 30.41 A C

ATOM 380 O ILE A 12519.799 21.81325.900 1.0D 29.68 A O

ATOM 381 N PHE A 12617.618 21.290_ 25.9281.00 30.30 A N

ATOM 382 CA PHE A 12617.356 22.04824.718 1.00 31.72 A C

ATOM 383 CB PHE A 12615.903 21.$7124.261 1.00 30.84 A C

ATOM 384 CG PHE A 12615.709 20.76423.267 1.00 29.33 A C

ATOM 385 CD1PHE A 12616.076 19.45723.579 1.00 27.14 A C
ATOM 386 CD2PHE A 12615.139 21.02622.0_261.00 28.45 A C

ATOM 387 CE1PHE A 12615.883 18.43222.681 1.00 26.37 A C
ATOM 388 CE2PHE A 12614.936 19.99621.109 1:00 29.21 A C
ATOM 389 CZ PHE A 12615.312 18.69221.442 1.00 27.93 A C

ATOM 390 C PHE A 12617.646 23.53024.965 1.00 33.28 A C

ATOM 391 O PHEA 12618.243 24.19124.115 1.00 32.31 A O

ATOM 392 N GLNA 12717.225 24.04126.122 1.00 35.44 A N

ATOM 393 CA GLNA 12717.464 25.44626.481 1.00 39.58 A C

ATOM 394 CB GLNA 12716.814 25,80627.821 1.00 41,42 A C

ATOM 395 CG GLN A 12715.327 26.08027.787 1,00 48:34 A C

ATOM 396 CD GLN A 12715.001 27.52427.429 1.00 51.71 A C
ATOM 397 OE1GLN A 12715.519 28.46428.048 1.00 55.77 A O

ATOM 398 NE2GLN A 12714.131 27.70826.441 1.00 51.19 A N
ATOM 399 C GlN A 12718.949 25.74726.611 1.40 39.96 A C

ATOM 400 O GLN A 12719.443 26.71626.042 1.00 41.19 A O

ATOM 401 N GLU A 12819.661 24.92827.374 1.00 40.45 A N

ATOM 402 CA GLU A 12821.078 25.17527.575 1.00 41.56 A C

ATOM 403 CB GLU A 12821.661 24.19728.592 1.00 43.84 A C

ATOM 404 CG GLU A 12823.146 24.45028.849 1.00 48.12 A C

ATOM 405 CD GLU A 12823.575 24.07530.250 1.00 49.95 A C

ATOM 406 OE1GLU A 12823.159 24.76631.211 1.00 51.99 A O

ATOM 407 OE2GLU A 12824.323 23,08630.384 1.00 51.57 A O
ATOM 408 C GLU A 12821.875 25.12126.284 1.00 40.66 A C

ATOM 409 O GLU A 12822.773 25.94226.070 1.00 41.46 A O

ATOM 410 N ARG A 12921.552 24.15325.42$ 1.00 38.84 A N

ATOM 411 CA ARG A 12922.225 24.01124.143 1.00 36.25 A C

ATOM 412 CB ARG A 12922.128 22.57223.645 1.00 36.53 A C

ATOM 413 CG ARG A 12922.973 21.60624.432 1.00 37.08 A C

ATOM 414 CD ARG A 12922.973 20.24523.784 1.00 39.71 A C

ATOM 415 NE ARG A 12923.945 19.35324.406 1.00 4129 A N

ATOM 416 CZ ARG A 12925.259 19.54724.364 1.00 43.21 A C

ATOM 417 NH1ARG A 12925.744 20.60523.723 1.00 44.30 A N

ATOM 418 NH2ARG A 12926.087 18.69324.966 1.00 42,88 A N

ATOM 419 C ARG A 12921.610 24.96423.114 1.00 35.32 A C

ATOM 420 O ARG A 12921.954 24.91621.929 1.00 33.95 A O

ATOM 421 N ASP A 13020.6$9 25.80923.583 1.00 33.36 A N

ATOM 422 CA ASP A 13020.028 26.81622.752 1.00 34.52 A C

ATOM 423 CB ASP A 13021.065 27,$7622.359 1.00 36.65 A C

ATOM 424 CG ASP A 13D20.442 29.16621.881 1.00 40.06 A C

ATOM 425 OD1ASP A 13019.462 29.63522.503 1.00 41.63 A O

ATOM 426 OD2ASP A 13020.953 29.72420.887 1.00 43.01 A O

ATOM 427 C ASP A 13019.368 26.22521.502 1.00 32.95 A C

ATOM 428 O ASP A 13019243 26,89720:480 1.00 33.04 A O

ATOM 429 N LEU A 13118.928 24.97521.601 1.00 31.57 A N

ATOM 430 CA LEU A 13118.312 24.27320.478 1.00 31.34 A C

ATOM 431 CB LEU A 13118.159 22.78020.822 1.00 30.04 A C

ATOM 432 CG LEU A 13119.473 21.99821.015 1.00 30.44 A C

ATOM 433 CD1LEU A 13119.156 20.58521.457 1.00 31.04 A C

ATOM 434 CD2LEU A 13120.275 21.95519.708 1.00 28.32 A C

ATOM 435 C LEU A 13116.975 24.84319.982 1.00 31,62 A C

ATOM 436 O LEU A 13116.660 24.70218.802 1.00 31.29 A O

ATOM 437 N LEU A 13216.198 25.47820.863 1.00 30.97 A N

ATOM 438 CA LEU A 13214.916 26.04720.458 1.00 32,09 A C

ATOM 439 CB LEU A 13214.080 26.46221.674 1.00 30.21 A C

ATOM 440 CG LEU A 13213.587 25.31422.550 1.00 31.86 A C

ATOM 441 CD1LEU A 13214.542 25.14123.736 1.00 30.70 A C

ATOM 442 CD2LEU A 13212.162 25.61123.056 1.00 31.59 A C

ATOM 443 C LEU A 13215.071 27.24319.523 1.00 32,39 A C

ATOM 444 O LEU A 13214.338 27.36018.541 1.00 33.30 A O

ATOM 445 N LYS A 13316.007 28.13819.827 1.00 33.51 A N

ATOM 446 CA LYS A 13316.227 29.29718.968 1.00 33,64 A C

ATOM 447 CB LYS A 13317,079 30.35119,675 1.00 35.69 A C

ATOM 448 CG LYS A 13316.293 31.15020.715 1.00 40.56 A C

ATOM 449 CD LYS A 13317.098 32.29121.346 1.00 42.55 A C

ATOM 450 CE LYS A 13316.193 33.16722.225 1.00 45.78 A C

ATOM 451 NZ LYS A 13316.924 34.30122.882 1.00 48.1 A N
S

ATOM 452 C LYS A 13316.901 28.88217.671 1.00 32:69 A C

ATOM 453 O LYS A 13316.536 29.35116.613 1.00 33.21 A O

ATOM 454 N THR A 13417.868 27.97717.750 1.00 31,65 A N

ATOM 455 CA THR A 13418,580 27.53216.559 1.00 29.79 A C

ATOM 456 CB THR A 13419.734 26.59816.945 1.00 29.39 A C

ATOM 457 OG1THR A 13420.674 27.32617.739 1.00 29.93 A O

ATOM 458 CG2THR A 13420.443 26.06115.710 1.00 29.19 A C

ATOM 459 C THR A 13417.680 26.82815.548 1.00 30.05 A C

ATOM 460 O THR A 13417.846 26.98814.329 1.0D 28.15 A 0 ATOM 461 N PHE A 13516.718 26.058-16.047 1.00 30.03 A N

ATOM 462 CA PHE A 13515.824 25.34215.153 1.00 30.31 A C
ATOM 463 CB PHE A 13515.855 23.85715.501 1.00 30.96 A C

ATOM 464 CG PHE A 13517.194 23.22615.255 1.00 31.92 A C

ATOM 465 CD1PHEA 13517.672 23.07513_.9571.00 8'1.52A C

ATOM 466 CD2_ A 13518.009 22.84516.319 1.0_0 31.99A C
PHE

ATOM 467 CE1PHEA 13518.944 22.55713.716 1.00 32.41A C

ATOM 468 CE2PHEA 13519.282 22.32616.096 1.00 31.62A C

ATOM 469 CZ PHEA 13519.754 22.18214.789 1.00 33.58A C

ATOM 470 C PHEA 13514.399 25.88515.130 1.00 30.78A C

ATOM 471 O PHEA 13513,493 25.24514.585 1.00 30.06A O

ATOM 472 N LYSA 13614.230 27.08815.687 1.00 30.32A N

ATOM 473 CA LYSA 13612.937 27.76115.760 1.00 30.86A C

ATOM 474 CB LYSA 13612.594 28.46914.428 1.00 31.15A C

ATOM 475 CG LYSA 13fi13.595 29.56014.031 1.00 33.42A C

ATOM 476 CD LYSA 13614.772 28.93013.276 1.00 37.59A C

ATOM 477 CE LYSA 13616.056 29,79913.244 1.00 38.69A C

ATOM 478 NZ LYSA 13617.108 29.20612.319 1.00 33.41A N

ATOM 479 C LYSA 13611,815 26.80916,164 1.00 29.71A C

ATOM 480 O LYSA 13610.806 26.66615.472 1.00 30.66A O

ATOM 481 N ILEA 13712,014 26.16017.302 1.00 29.74A N

ATOM 482 CA ILEA 13711.046 25.22917.859 1.00 28.75A C

ATOM 483 CB ILEA 13711.749 24.08018.624 1.00 29.67A C

ATOM 484 CG2ILEA 13710.705 23.16119.279 1.00 26.49A C

ATOM 485 CG1ILEA 13712.679 23.31117.673 1.00 29.88A C

ATOM 486 CD1ILEA 13713.532 2 18.378 1.00 27.99A C
2.279 ATOM 487 C ILEA 13710.201 _ 18.869 1.00 28.90A C
25.991 ATOM 488 O ILEA 13710.723 26.49319.877 1.00 29.07A O

ATOM 489 N PROA 1388.892 26.12018.609 1.00 28.68A N
ATOM 490 CD PROA 1388.155 25.93617.347 1.00 27.52A C
ATOM 491 CA PROA 1388.108 26. 19.612 1.00 28.58A C

ATOM 492 CB PROA 1386.741 _ 18.951 1_.00 27.35A C
_ 27,021 ATOM 493 CG PROA 1386:750 26.08117.768 1.00 28.65A C' ATOM 494 C PROA 1388.071 26.04220,914 1.00 29.78A C

ATOM 495 O PROA 1387.940 24.81720.880 1.00 30.68A O

ATOM 496 N VALA 1398.219 26.72022.051 1.00 30.81A N

ATOM 497 CA VALA 1398.233 26.05223.344 1.00 32.31A C

ATOM 498 CB VALA 1398.333 27.07324.523 1.00 33.30A C

ATOM 499 CG1VALA 1399.626 829 24.435 1.00 35.40A C
27.

ATOM 500 CG2VALA 1397.168 _ 24.494 1.00 33.02A C
28.049_ ATOM 501 C VALA 1397.033 25.13823.598 1.00 33.26A C

ATOM 502 O VALA 1397.203 24.00324.030 1.00 32.12A O

ATOM 503 N ASPA 1405.830 25,64323.337 1.00 34.32A N

ATOM 504 CA ASPA 1404.599 24.89123.557 1.00 35.87A C

ATOM 505 CB ASPA 1403.400 25.71023.087 1.00 42.04A C

ATOM 506 CG ASPA 1403.269 27.00123.841 1.0D 47.68A C

ATOM 507 OD1ASPA 1404.153 27.25124.698 1.00 50.99A O

ATOM 508 OD2ASPA 1402.298 27.76123.587 1.00 50.99A O

ATOM 509 C ASPA 1404,596 23.56822.827 1.00 32.97A C

ATOM 510 O ASPA 1404.162 22.54723.367 1.00 30.40A 0 ATOM 511 N THRA 1415,058 23.62021.582 1.00 30.48A N

ATOM 512 CA THRA 1415.137 22.45720.715 1.00 29.29A C

ATOM 513 CB THRA 1415,588 22.88219,293 9.00 30.83A C

ATOM 514 OG1THRA 1414.768 23.97618.842 1.00 33.17A O

ATOM 515 CG2THRA 1415.461 21.73318.313 1.00 29.96A C

ATOM 516 C THRA 1416.154 21.48421.324 1.00 28.32A C

ATOM 517 0 THRA 1415.917 20.27321.335 1.00 25.92A 0 ATOM 518 N LEUA 1427.264 22.01721.851 1.00 25.89A N

ATOM 519 CA LEUA 1428.298 21.17222.454 1.00 25.82A C

ATOM 520 CB LEUA 1429.557 21.98222.795 1.00 24.46A C

ATOM 521 CG LEUA 14210,664 21.13123.451 1.00 25.92A C

ATOM 522 CD1LEUA 14211,089 20.05622.485 1.00 24.05A C

ATOM 523 CD2LEUA 14211.874 21.97423.858 1.00 23.95A C

ATOM 524 C LEUA 1427.782 20.47423.716 1.00 25.24A C

ATOM 525 O LEUA 1427.935 19.26723.876 1.00 26.03A O

ATOM 526 N ILEA 1437,167 21.23624.609 ' 1.00__24.59A N

ATOM 527 CA ILEA 1436.628 20.67825.834 1.00 24.78A C

ATOM 528 CB ILEA 1436.078 21.79826.748 1.00 26.49A C

ATOM 529 CG2ILEA 1435.468 21.19228.020 1.00 25.05A C

ATOM 530 CG1ILEA 1437.231 22.75027.115 1.00 27.38A C

ATOM 531 CD1ILEA 1436.857 23.90628.025 1.00 31.42A C

ATOM 532 C ILEA 1435.543 19.65325,529 1.00 2522 A C

ATOM 533 O ILEA 1435.533 18.56926.095 1.00 _27.25A O

ATOM 534 N THRA 1444.648 19.98524.609 1.00 24.44A N

ATOM 535 CA THRA 1443,576 19.07824.239 1.00 23.99A C

ATOM 536 CB THRA 1442.623 19.77123.227 1.00 23.96A C

ATOM 537 OG1THRA 1442.060 20,94823.840 1.00 22.69A O

ATOM 538 CG2THRA 1441.504 18.84022.814 1.00 20.48A C
ATOM 539 C THRA 1444.121 17.75923.658 1.00 25.11A C

ATOM 540 O THRA 1443.658 16.66524.009 1.00 23.35A O

ATOM 541 N TYRA 1455.103 17,85822.766 1.00 24.95A N

ATOM 542 CA TYRA 1455.675 16.66122.195 1.00 22.82A C

ATOM 543 CB TYRA 1456,730 16.97921.144 1.00 20.94A C

ATOM 544 CG TYRA 1457.443 15.716_2_0.68_9_ 1_00_19.71_R C
ATOM 545 C01TYRA 1456.847 14,85619.775 1.00 18.51A C

ATOM 546 CE1TYRA 1457.460 13.66519.391 1.00 18.01A C
ATOM 547 CD2TYRA 1458.684 15.35421.223 1.00 19.42A C

ATOM 548 CE2TYRA 1459.316 14.15420.843 1.00 20.05A C
ATOM 549 CZ TYRA 1458.691 13.32319.921 1.00 19.64A C
ATOM 550 OH TYRA 1459.304 12.17419.486 1.00 18.29A O

ATOM551 C TYRA 1456.357 15.83123.277 1.00 23.49 A C

ATOM552 0 TYRA 1456.146 14.61623.361 1.00 21.64 A O

ATOM553 N LEUA 1467.195 16.495_ 24.0731.00 22.83 A N

ATOM554 CA LEUA 1467.936 15.81525.132 1.00 24.47 A C

ATOM555 CB LEUA 1468.761 16.82425.947 1.00 21.65 A C

ATOM556 CG LEUA 1469.908 17.49525.165 1.00 2D.94 A C

ATOM557 CDtLEUA 14610.727 18.47326.027 1.00 16.46 A C

ATOM558 CD2LEUA 14610.790 16.39024.630 1.00 18.71 A C

ATOM559 C LEUA 1466.989 15.03026.035 1.00 25.78 A C

ATOM560 O LEUA 1467.208 13.84826.303 1.00 26.56 A O
ATOM561 N META 1475.926 15.68826.476 1.00 26.10 A N

ATOM562 CA META 1474.952 15.053_ T 1.0026.33 A C
27.338 ATOM563 CB META 1473.898 16.06027.773 1.00 26.28 A C

ATOM564 CG META 1474.375 17.03528.820 1.00 29.31 A C

ATOM565 SD META 1473,101 18.25029.182 1.00 37.54 A S

ATOM566 CE META 1473.448 18.53530.884 1.00 36.43 A C

ATOM567 C META 1474.286 13.91326.603 1.00 26.65 A C

ATOM568 O META 1473.983 12.86827.184 1.00 26.59 A O

ATOM569 N THRA 1484.044 14.11425.316 1.00 26.08 A N

ATOM570 CA THRA 1483.408 13.06924.543 1.00 25.87 A C

ATOM571 CB THRA 1482.969 13.60023.171 1.00 24.99 A C

ATOM572 OG1THRA 1482.045 14.68823.361 1.D0 24.61 A O

ATOM573 CG2THRA 1482.304 12.51522.376 1.00 21,54 A C

ATOM574 C THRA 1464.392 11.90124.404 1.00 26.75 A C

ATOM575 O THRA 1484,015 10.73824.533 _1.00 26,17 A O

ATOM576 N tEUA 1495.662 12.215_ 1:00 27.02 A N
ATOM577 CA LEUA 1496.664 11.16724.181 1.00 27.80 A G
24.051 ATOM578 CB LEUA 1498.030 11.76023.709 1.0D 26.05 A C

ATOM579 CG LEUA 1499.141 10.71423.597 1.00 26.66 A C
ATOM580 CD1LEUA 1498.852 9.797 22.409.1.00 25.72 A C

ATOM581 CD2LEUA 14910.495 11.40523.428 1.00 25.75 A C

ATOM582 C LEUA 1496.760 10.40425.368 1.00 28.25 A C

ATOM583 O LEUA 1496,722 9.170 25.392 1.00 27,53 A O

ATOM584 N GLUA 1506.881 11.14326.462 1.00 27.61 A N

ATOM585 CA GLUA 1508.989 10.51927.769 1.00 28.78 A C

ATOM586 CB GLUA 1507,263 11.59928.829 1.00 30.04 A C

ATOM587 CG GLUA 1507.488 11.06430.245 1.00 31.58 A C
, ATOM588 CD GLUA 1508.394 11.963___31.077__1.0033.34_A C

ATOM589 OE1GLUA 1508.26D 13.21230.975 1.00 32,52 A O
ATOM590 OE2, A 1509.234 11.41631.837 1.00 31.84 A O
GLU

ATOM591 C GLUA 1505.733 9.689 28.102 1.00 28,00 A C

ATOM592 O GLUA 1505.826 8.600 28.675 1.00 27.35 A 0 ATOM593 N ASPA 1514.565 10.19127.718 1.00 27.97 A N
ATOM594 CA ASPA 1513.312 9.478 27.948 1.00 28,06 A C

ATOM595 CB ASPA 1512.131 10.25727.371 1.00 30.58 A C
ATOM596 CG ASPA 1511.683 11.40528.253 1.D0 32,54 A C

ATOM597 ODtASPA 1510.951 12.29527.741 1,00 33.02 A O
ATOM598 OD2ASPA 1512.048 11.40529.449 1.00 31.81 A O
ATOM599 C ASPA 1513.347 8.124 27.253 1.00 28.57 A C

ATOM600 O ASPA 1512.589 7.230 27.608 1.0D 29.82 A O
ATOM601 N HISA 1524.201 7.973 26.244 1.00 26.56 A N
ATOM602 CA HISA 1524.254 6.708 25.532 1.00 27.15 A C

ATOM603 CB HISA 1524.381 6.936 24.026 1.00 26.40 A C
ATOM604 CG HISA 1523.091 7.358 23.392 1.D0 27.65 A C

ATOM605 CD2HISA 1522.275 6.717 22.520 1.00 25.84 A C
ATOM606 ND1HISA 1522.459 8.542 23.712 1.00 24.40 A N
ATOM607 CEtHISA 1521.309 8.610 23.066 1.00 26,84 A C

ATOM608 NE2HISA 1521.174 7.515 22.336 1.00 27.16 A N
ATOM6O9 C HISA 1525.271 5.706 26.026 1.00 26.95 A C

ATOM610 O HISA 1525,456 4.663 25.425 1.00 27.46 A O

ATOM611 N TYRA 1535.943 6.034 27.121 1.00 28.62 A N
ATOM612 CA TYRA 1536.835 5.077 27.763 1.00 28.81 A C

ATOM613 CB TYRA 1537.972 5.780 28.497 1.00 25,85 A C

ATOM614 CG TYRA 1539.162 6.010 27.613 1.00 26.45 A C
ATOM615 CD1TYRA 1539.190 7.059 26.690 1.00 24,55 A C

ATOM616 CE1TYRA 15310.269 7.213 25.820 1.00 24.63 A C
ATOM617 CD2TYRA 15310.236 5.131 27.643 1.00 26.98 A C

ATOM618 CE2TYRA 15311.307 5.272 26.781 1.00 25.58 A C

ATOM619 C2 TYRA 15311.321 6.306 25.875 1.00 23.91 A C
ATOM620 OH TYRA 15312.382 6.401 25.016 1.00 22.28 A O

ATOM621 C TYRA 1535.884 4.405 28.774 1.00 30.31 A C
ATOM622 O TYRA 1534.913 5.035 29.225 1.00 28.86 A O
ATOM623 N HISA 1546.136 3.144 29.122 1.00 32.58 A N

ATOM624 CA HISA 1545.252 2.436 3D.062 1.00 34.81 A C
ATOM625 CB H A 1545_.203 ___0.94_029.725 1.00 33.50 A C
IS

ATOM626 CG HIS_ 154_4,793__0.646 28.312 _ 34.74 A C
A 1.00 ATOM627 CD2HISA _ 4.568 _ 27.256 1.00 34.45 A C
ATOM628 ND1HISA 1544.585 1.465 27.850 1.00 34.98 A N
ATOM629 CE1HISA 1544.252 -0.63526.571 1,00 35,49 A C
ATOM630 NE2HISA 1544.235 -0.59326.187 1.00 33.22 A N
ATOM631 C HISA 1545.639 0.671 31.534 1.00 36.34 A C
154 2.611 ATOM632 O HISA 1546.757 2.281 31.944 1.00 37.37 A O
ATOM633 N ALAA 1554.705 3.133 32.323 1.00 37.44 A N
ATOM634 CA ALAA 1554.929 3.326 33.748 1.00 39.05 A C

ATOM635 CB ALAA 1553.820 4.190 34.337 1.00 37.37 A C
ATOM636 C ALAA 1554.983 1.968 34,463 1.00 40.52 A C

ATOM637 O ALAA 1555.621 1.835 35.507 1.00 42.72 A O
ATOM638 N ASPA 156_ 4.3280.960 33.894 1.00 41.11 A N
ATOM639 CA ASPA 1564.314 -0.37734,490 1.00 42.47 A C

ATOM640 CB ASPA 1563,001 -1.09634.156 1.00 44.68 A C

ATOM641 CG ASPA 1562.819 -1.33232.668 1.00 47.86 A C
ATOM642 OD1ASPA 1563.008 -0.37831.878 1.00 50.47 A O

ATOM643 OD2ASPA 1562.471 -2.47032.285 1.00 50.30 A O

ATOM644 C ASPA 1565.495 -1.23734.040 1.00 41.74 A C
ATOM645 0 ASPA 1565.438 -2.46934.090 1.00 41.25 A O
ATOM646 N VALA 1576.557 -0.58033.582 1.00 40.02 A N

ATOM647 CA VALA 1577.767 -1.26633.143 1.0D 37.69 A C

ATOM648 CB VALA 1578.101 -9.91331.673 1.00 38.72 A C
ATOM649 CG1VALA 1579.588 -1.12631.391 1.00 39.68 A C
ATOM650 CG2VALA 1577.258 -1.78530.738 1.00 37.18 A C

ATOM651 C VALA 1578.840 -0.76634.091 1.00 37.22 A C

ATOM652 O VALA 1579.026 0.440 34.241 1.00 37.1D A O
ATOM653 N ALAA 1589.538 -1.69134.738 1.00 36.23 A N
ATOM654 CA ALAA 15810.548 -1.33435.727 1.00 35.20 A C

ATOM655 CB ALAA 15810.983 -2.58636.486 1.00 36.12 A C

ATOM656 C ALAA 15811.767 -0.61935.183 1.00 34.84 A C
ATOM657 O ALAA 15812.254 0.338 35.783 1.00 34.73 A O

ATOM658 N TYRA 15912.264 -1.08534.046 1.00 34.63 A N

ATOM659 CA TYRA 15913.451 -0.49333.451 1.00 33.78 A C

ATOM660 CB TYRA 15914.448 -1.59633.109 1.00 32.62 A C
ATOM661 CG TYRA 15915.801 -1.07532.672 1.00 33.47 A C
ATOM662 CD1TYRA 15916.773 -0.73233.610 1.00 31.55 A C

ATOM663 CE1TYRA 15918,019 -0.25133.211 1.00 31.19 A C

ATOM664 CD2TYRA 15916.108 -0.92031.315 1.00 31.50 A C

ATOM665 CE2TYRA 15917.350 -0.43730.909 1.00 31.15 A C

ATOM666 CZ TYRA 15918.303 -0.10631.859 1.00 31.46 A C

ATOM667 OH TYRA 15919.546 0.348 31.459 1.00 30.33 A O

ATOM668 C TYRA 159. 13.2170.376 32.205 1.0D 32.55 A C

ATOM669 O TYRA 15913.495 1.572 32.214 1.00 31.53 A 0 ATOM670 N HISA 16012.713 -0.23231.138 1.00 32,51 A N

ATOM671 CA HISA 16012.502 0.484 29.883 1.00 31,56 A C

ATOM672 CB HISA 16012.337 -0.52128.750 1,00 31.20 A C

ATOM673 CG HISA 16013.537 -1.39328.553 1.00 33.12 A C

ATOM674 CD2HISA 16014.731 -1.14427.964 1.00 32.39 A C
-ATOM675 ND1HIS' 16013.607 -2.68629,027 1.00 33.31 A N
A

ATOM676 CE1HIS' 16014.790 -3.19528.742 1.00 33.77 A C
A

ATOM677 NE2HISA 16015.492 -2.27928.098 1.00 34.81 A N

ATOM678 C HISA 16011.348 1.471 29.903 1.00 30.57 A C

ATOM679 O HISA 16010.371 1.339 29.166 1.00 29.63 A O

ATOM680 N ASNA 16111.503 2.487 30.740 1.00 30.41 A N

ATOM681 CA ASNA 16110.500 3.512 30.916 1.00 30.58 A C

ATOM682 CB ASNA 1619.902 3.398 32.318 1.00 32.01 A C

ATOM683 CG ASNA 16110.968 3.380 33.408 1.00 34.02 A C

ATOM684 OD1ASNA 16111.706 4.347 33.585 1.00 36.03 A O

ATOM685 ND2ASNA 16111.053 2.271 34.137 1.00 35.D2 A N

ATOM686 C ASNA 16111.099 4.900 30.712 1.00 30.44 A C

ATOM687 O ASNA 16112,258 5.036 30.314 1.00 29.86 A O

ATOM688 N ASNA 16210.304 5.924 31.011 1.00 29.70 A N

ATOM689 CA ASNA 16210.729 7.296 30.840 1.00 30.11 A C

ATOM690 CB ASNA 1629.568 8:248 31,143 1.00 31.77 A C

ATOM691 CG ASNA 1629.035 8.097 32.553 1.00 31.65 A C

ATOM692 OD1ASNA 1628.738 6.991 33.002 1.00 33.89 A O

ATOM693 ND2ASNA 1628.897 9.214 33.254 1.00 29.14 A N

ATOM694 C ASNA 16211.946 7.678 31,662 1.00 30.37 A C

ATOM695 O ASNA 16212.677 8.601 31.283 1.00 30.43 A O

ATOM696 N ILEA 16312.178 6.987 32.779 1.00 29.92 A N

ATOM697 CA ILEA 16313.338 7.310 33.600 1.00 28,83 A C
ATOM698 CB ILEA 16313.285 6.620 34.987 1.00 31.11 A C
ATOM699 CG2ILEA 16314.396 7.186 35.896 1.00 29.73 A C

ATOM700 CG1ILEA 16311.925 6.876 35.651 1.00 28.55 A C

ATOM701 CD1ILEA 16311.832 6.361 37,D71 1.00 28.57 A C

ATOM702 C ILEA 16314.597 6.884 32.845 1.00 28.69 A C

ATOM703 O ILEA 16315.549 7.649 32.763 1.00 28.59 A O

ATOM704 N HISA 16414.593 5.677 32.282 1.00 28.81 A N

ATOM705 CA HISA 16415.732 5.182 31.496 1.00 29.72 A C

ATOM706 CB HISA 16415.464 3.742 31,012 1.00 30.68 A C

ATOM707 CG HiSA 164_ 16.4383.241 29.978 1.00 32.06 A C

ATOM708 CD2HISA 16416.240 2.796 28.712 1.00 30.30 A C

ATOM7D9 ND1HISA 16417,793 3.136 30,213 1.00 32.38 A N

ATOM710 CE1HISA 16418,387 2.648 29.137 1.00 32.61 A C
ATOM711 C HISA 16415.956 6.118 30.297 1.00 30.48 A C

ATOM712 O HISA 164_17.091 6.426 29.949 1.00 32.20 A O

ATOM713 NE2HISA 16417.468 2.432 28,209 1.00 33.98 A N

ATOM714 N ALAA 16514.875 6.582 29,674 1.00 30.45 A N

ATOM715 CA ALAA 16514.994 7.501 28.541 1,00 28.45 A C

ATOM716 CB ALAA 165_13.630 7.776 27.938 1.00 27.26 A C
' ATOM717 C ALAA 16515.642 8.813 28.971 1.00 28.25 A C

ATOM718 O ALAA 16516.558 9.309 28.307 _ 27.73 A O

.00 ATOM719 N ALAA 16615.159 9.386 30.069 _ 28.37 A N
1.00' ATOM720 CA ALAA 16615.728 10.64430.568 1.00 29.12 A C

ATOM721 CB ALAA 16614.987 11.10831.814 1.00 28.00 A C
ATOM722 C ALAA 16617.203 t 0.43030.894 1 00 29 A C
~ ~ ( ~ T 48 ATOM 723 0 ALAA 16618.044 11,26830.5901.00 ~ 27.82A 0 ATOM 724 N ASPA 16717.491 9.277 31.5011.00 31.70 A N

ATOM 725 CA ASPA 16718.839 8.881 31.8951.00 31.54 A C

ATOM 726 CB ASPA 16718.782 7.500 32.5731.00 33.06 A C

ATOM 727 CG ASPA 16720.137 7.038 33.1231.00 33.69 A C

ATOM 728 OD1ASPA 16720.901 7.875 33.6551.00 32.40 A O

ATOM 729 OD2ASPA 16720.420 5.820 33.0401.00 34.99 A O

ATOM 730 C ASPA 16719.745 8.841 30.6701.00 31.06 A C

ATOM 731 O ASPA 16720.832 9.426 30.6651.00 31.21 A O

ATOM 732 N VALA 16819.280 8.169 29.6221.00 29.80 A N

ATOM 733 CA VALA 16820.049 8.048 25.3931.00 29.08 A C

ATOM 734 CB VALA 16819.375 7.036 27.4421.00 29.55 A C

ATOM 735 CG1VALA 16820.082 7.016 26.0941.00 26.88 A C

ATOM 736 CG2VALA 16819.414 5.648 28.0891.00 27.26 A C

ATOM 737 C VALA 16820.259 9.392 27.6981.00 28.55 A C

ATOM . O VALA 16821.310 9.628 27.1061.00 28.22 A O

ATOM 739 N VALA 16919.264 10.27127.7801.00 28.68 A N

ATOM 740 CA VALA 16919.349 11.61027.1871.00 28.39 A C

ATOM 741 CB VALA 16917.979 12.38327.2961.00 26.66 A C

ATOM 742 CG1VALA 16918.200 13.56527.1951.00 25.94 A C

ATOM 743 CG2VALA 16917.042 11.95026.2031.00 26.44 A C

ATOM 744 C VALA 16920.420 12.44127.8931.00 29.23 A C

ATOM 745 O VALA 16921.307 13.00027.2561.00 31.69 A O

ATOM 746 N GLN. 17020.331 12.51929.2141.00 30.24 A N
A

ATOM 747 CA GLN! 17021.271 13.30030.0081.00 30.84 A C
A

ATOM 748 CB GLN' 17020.815 13.31531.4641.00 28.82 A C
A

ATOM 749 CG GLNA 17021.589 14.26432.3601.00 29.87 A C

ATOM 750 CD GLNA 17022.722 13.57933.1181.00 29.09 A C

ATOM 751 OE1GLNA 17022.590 12.43333.5531.00 25.58 A O

ATOM 752 NE2GLNA 17023.828 14.29433.3031.00 27.93 A N

ATOM 753 C GLNA 17022.694 12.76029.9031.00 31.83 A C

ATOM 754 O GLNA 17023.663 13.53229.9381.00 33.37 A O

ATOM 755 N SERA 17122.51_1_11.44229.7731.00 31.15 A N

ATOM 756 CA SERA 17124.111 10.78729.6551.00 32.73 A C

ATOM 757 CB SERA 17123.961 9.270 29.8241.00 32.54 A C

ATOM 758 OG SERA 17123.635 8.938 31.1641.00 34.43 A O

ATOM 759 C SERA 17124.767 11.09725.3081.00 32.90 A C

ATOM 760 0 SERA 17125.985 11.31328.2321.00 33.11 A O

ATOM 761 N THRA 17223.963 11.08527.2471.00 31.83 A N

ATOM 762 CA THRA 17224.462 11.40525.9151.00 31.37 A C

ATOM 763 CB THRA 17223.378 11.21824.8351.00 31.00 A C

ATOM 764 OG1THRA 17223.029 9.837 24.7411.00 28.85 A O

ATOM 765 CG2THRA 17223.580 11.70923.4771.00 30.56 A C

ATOM 766 C THRA 17224.853 12.87725.9601.00 31.05 A C

ATOM 767 0 THRA 17225.896 13.25925.4491.00 31.40 A O

ATOM 768 N HISA 17324.004 ' 13.69126.5881.00 31.94 A N

ATOM 769 CA HISA 17324.259 15.12226.7391.00 33.24 A C

ATOM 770 CB HISA 17323.178 15.77027.6011.00 32.19 A C

ATOM 771 CG HISA 17323.487 17.18028.0051.00 35.34 A C

ATOM 772 CD2HISA 17323.579 17.75929.2261.00 34.86 A C

ATOM 773 ND1HISA 17323.753 18.17827.0901.00 37.14 A N

ATOM 774 CE1HISA 17323.998 19.30827.7311.00 33.89 A C

ATOM 775 NE2HISA 17323.899 19.08129.0261.00 33.22 A N

ATOM 776 C HISA 17325.633 15.37227.3671.00 34.21 A C

ATOM 777 O HISA 17326.381 16.23226.9041.00 34.38 A 0 ATOM 778 N VALA 17425.966 14.62528.4201.00 35.22 A N

ATOM 779 CA VALA 17427.268 14.79629.0741.00 36.14 A C

ATOM 780 CB VALA 17427.341 14.03430.4201.00 37.02 A C

ATOM 781 CG1VALA 17428.779 14.01530.9321.00 36.14 A C

ATOM 782 CG2VALA 17426.440 14.70431.4451.00 36.20 A C

ATOM 783 C VALA 17428.390 14.29828.1681.00 36.12 A C

ATOM 784 O VALA 17429.471 14.87628.1221.00 35.32 A O

ATOM 785 N LEUA 17528.132 13.21927.4451.00 36.34 A N

ATOM 786 CA LEUA 17529.140 12.69126.5511.00 37.70 A C

ATOM 787 CB LEUA 17528.672 11.36925.9521.00 37.56 A C

ATOM 788 CG LEUA 17528.830 10.21426.9381.00 38.18 A C

ATOM 789 CD1LEUA 17528.244 8.942 26.3701.00 36.80 A C

ATOM 790 CD2LEUA 17530.313 10.03427.2401.00 38.37 A C

ATOM 791 C LEUA 17529.453 13.69825.4491.00 39.15 A C

ATOM 792 0 LEUA 17530.627 13.91625.1261.00 38.87 A O

ATOM 793 N LEUA 17628.412 14.32624.8941.00 38.05 A N

ATOM 794 CA LEUA 17628,604 15.30623.8301.00 39.08 A C

ATOM 795 CB LEUA 17627.262 15.86323.3511.00 38 A C

ATOM 796 CG LEUA 17626.321 14.95122.5721.00 . A C
37.76 ATOM 797 CD1LEUA 17624.955 15.62322.5251.00 38.43 A C

ATOM 798 CD2LEUA 17626.862 14.67521.1731.00 37 A C

ATOM 799 C LEUA 17629.496 16.46824.2571.00 . A C
39.93 ATOM 800 O LEUA 17630.231 17.00623.4371.00 39.77 A O

ATOM 801 N SERA 17729.431 16.84125.5351.00 41.20 A N

ATOM 802 CA SERA 17730.227 17.94926.0711.00 43 A C

ATOM 803 CB SERA 17729.591 18.49727.3551.00 . A C

ATOM 804 OG SERA 17728.267 18.94727.1381.00 . A O

ATOM 805 C SERA 17731.679 17.59226.3871.00 . A C
44.17 ATOM 806 0 SERA 17732.415 18.41126.9511.00 43 A O

ATOM 807 N THRA 17832.106 16.38526 1 . A N

ATOM 808 CA THRA 17833 15 . . .

. . . 1.00 47.64 A C

ATOM809 CB THRA 17833.694 14.48726.062 1.00 48.66 A C

ATOM810 OGtTHRA 17834.695 13.98726.954 1.00 51.04 A O

ATOM811 CG2THRA 17834.136 14.24824.629 1.00 48.40 A C

ATOM812 C THRA 17834,525 16.80925.562 1.00 47.98 A C

ATOM813 O THRA 17834.340 17.12724.382 1.00 47.40 A O

ATOM814 N PROA 17935.632 17.17526.237 1.00 48.95 A N

ATOM815 CD PROA 17935.864 16.87827.666 1.00 49,03 A C

ATOM816 CA PROA 17936.744 17.96025.675 1.00 49.31 A C

ATOM817 GB PROA 17937.821 17.83826.750 1.0D 49,42 A C

ATOM818 CG PROA 17937.013 17.80328.020 1.00 49.26 A C

ATOM819 C PROA 17937.238 17.47324.313 1.00 49.65 A C

ATOM820 O PROA 17937,440 18.26823.398 1.00 50,08 A O

ATOM821 N ALAA 18037.417 16.16324.186 1.00 49.36 A N

ATOM822 CA ALAA 18037.902 15.55822.948 1.00 50.10 A C

ATOM823 CB ALAA 18038.193 14.07023.182 1.00 50.01 A C

ATOM824 C ALAA 18036.959 15.71321.752 1.00 50.88 A C

ATOM825 O ALAA 18037,355 15.48120.602 1.00 49.85 A O

ATOM826 N LEUA 18135.716 16.08822.011 1.00 50.88 A N

ATOM827 CA LEUA 18.134.755 16.24620.922 1.00 51.31 A C

ATOM828 CB LEUA 18133.540 15.35321.156 1.00 50.09 A C

ATOM829 CG LEUA 18133.865 13.86121.180 1.00 49.77 A C

ATOM830 CD1LEUA 18132.662 13.07721.675 1.00 49,87 A C

ATOM83t CD2LEUA 18134.278 13.41219.795 1:00 49.37 A C

ATOM832 C LEUA 18134.317 17.69220.787 1.00 51.32 A C

ATOM833 O lEUA 18133.479 18.01719.955 1,00 51.13 A O
;

ATOM834 N GLUA 18234.910 18.55421.603 1.00 51.72 A N
~

ATOM835 CA GLUA 18234.582 19.96621.598 1.00 52.42 A C

ATOM836 CB GLUA 18235;623 20.730__22.42_51,_0054.71 A C

ATOM837 CG GLUA 18235.093 21.98323.119 1.00 58.91 A C

ATOM838 CD GLUA 18236.007 22.46924.249 1.00 61,63 A C

ATOM839 OE1GLUA 18237,221 22.67624.002 1.00 62.75 A O
ATOM840 OE2GLUA 18235.509 22.64825.385 1.00 62.11 A O

ATOM841 C GLUA 18234.497 20.51620.167 1.00 52,23 A C

ATOM842 O GLUA 18235.392 20.30119.339 1.00 51.24 A O

ATOM843 N ALAA 18333.390 21.19919.885 1.00 51.07 A N

ATOM844 CA ALAA 18333.137 21.79818.580 1.00 49.90 A C

ATOM845 CB ALAA 18334.018 23.04718.409 1.00 50.45 A C

ATOM846 C ALAA 18333.306 20.87117.367 1.00 48.24 A C

ATOM847 O ALAA 18333.575 21.34416.260 1.00 48,84 A O

ATOM848 N VALA 18433.135 19.56817.557 1.00 45.89 A N

ATOM849 CA VALA 18433.272 18.62216.447 1.00 43,71 A C

ATOM850 CB VALA 18433.757 17.23016.918 1.00 44.17 A C
ATOM851 CGtVALA 18433.789 16.26115.738 1.00 44.54 A C

ATOM852 CG2VALA 18435.134 17.33017.528 1.00 43,83 A C

ATOM853 C VALA 18431.973 18.39715.678 1.00 42.73 A C
ATOM854 0 VALA 18431.978 18.29114.455 1.00 42.82 A O

ATOM855 N PHEA 18530.862 18.31116.395 1,00 40.30 A N

ATOM856 CA PHEA 18529.580 18.06215.757 1.00 38.68 A C
ATOM857 CB PHEA 18528.764 17.08816.615 1.00 39.34 A C

ATOM858 CG PHEA 18529.370 15.72116.716 1.00 38.88 A C
ATOM859 CD1PHEA 18529.394 14.87415.612 1.00 37.98 A C
ATOM860 CD2PHEA 18529.942 15.283___17_.9081.00 38.06 A C

ATOM861 CE1PHEA 185_29.979-13.611__15._693__1.00_36.94___A C
ATOM862 CE2PHEA 185__30.533__14.019_17.9_931_.00__37.12A C.
ATOM863 CZ PHEA 18530.550 13.18716.888 1,00 35.17 A C
ATOM864 C PHEA 1$528,785 19.33515.531 1.00 37.01 A C
ATOM865 O PHEA 18528.938 20.30616.260 1,00 37.37 A O

ATOM866 N THRA 18627.940 19.32414.508 1.00 35.59 A N
ATOM867 CA THRA 18627.091 20.47614.210 1.00 35.65 A C

ATOM868 CB THRA 18626.563 20.44012.769 1.00 34.01 A C

ATOM869 OG1THRA 18625.686 19.31512.627 1.00 35.08 A O

ATOM870 CG2THRA 18627.711 20.31811.766 1.00 31.32 A C

ATOM871 C THRA 18625.873 20.40115.125 1.00 36.37 A C

ATOM872 0 THRA 18625.604 19.35515.738 1.00 36.18 A O

ATOM873 N ASPA 18725.132 21.50115.214 1,00 36.39 A N

ATOM874 CA ASPA 18723.929 21.52516.034 1.00 35.54 A C
ATOM875 CB ASPA 18723.277 22.90415.990 1.00 36.58 A C
ATOM876 CG ASPA 18724.042 23.93816.786 1.00 37,47 A C

ATOM877 OD1ASPA 18724.327 23.69217.971 1.00 40,67 A 0 ATOM878 OD2ASPA 18724.347 25.00616.234 1.00 38.99 A O

ATOM879 C ASPA 18722.922 20.47915.553 1.00 34.22 A C
ATOM880 O ASPA 18722.178 19.91116.351 1.00 35.58 A O
ATOM881 N LEUA 18822.904 20.20714.254 1.00 33.11 A N

ATOM882 CA LEUA 18821.958 19.23413.734 1.00 33.43 A C
ATOM883 CB LEUA 18821.896 19.29712.204 1.00 32.16 A C
ATOM884 CG LEUA 18820.759 18.45511.609 1,00 33.64 A C

ATOM885 CD1LEUA 18819.414 19.02812.074 1.00 31.11 A C

ATOM886 CD2LEUA 18820.847 18.43110.077 1.00 31.88 A C
ATOM887 C LEUA 18822,295 17.81414.183 1.00 32.91 A C

ATOM888 O LEUA 18821.404 16.99814.397 1.00 33.06 A O
ATOM889_N GLUA 18923.586 17.52014.313 1.00 33,40 A N

ATOM890 CA GLUA 189_ 16.19614.751 1.00 32.23 A C
ATOM891 CB GLUA 18924.036 16.02714.410 1,00 34.03 A C
ATOM892 CG GLUA 18925.514 16.19112.922 1.00 35,83 A C
25.748 ATOM893 CD GLUA 18927.198 16.12412.546 1.0D 36.77 A C
ATOM894 OE1GLUA 18928.001 16.85313.158 1.00 37.50 A O

ATOM 895 OE2GLUA 18927.52515.352 11.6281.00 38.65 A O

ATOM 896 C GLUA 18923.79816.03 5 16.2491.00 30.62 A C

ATOM 897 O GLUA 18923.43314.961 16.7231.00 29.96 A O

ATOM 898 N ILEA 19024.00917.119 16.9821.00 27.92 A N

ATOM 899 CA ILEA 19023.77017.142 18.4151.00 27.52 A C

ATOM 900 CB ILEA 19024.20118.516 18.9831.00 27.58 A C

ATOM 901 CG2ILEA 19023.48918.812 20.2811.00 24.67 A C

ATOM 902 CG1ILEA 19025.73418.552 19.1051.00 27.04 A C

ATOM 903 CD1ILE; 19026.31619.949 19.2521.00 27.29 A C
A

ATOM 904 C ILEI 19022.26416.896 18.6411.00 27.06 A C
A

ATOM 905 0 ILEA 19021.87116.027 19.4251.00 26.14 A O

ATOM 906 N LEUA 19121.43317.659 17.9311.00 27.29 A N

ATOM 907 CA LEUA 19119.97917.520 18.0221.00 25.76 A C

ATOM 908 CB LEUA 19119.29518.438 17.0011.00 25.84 A C

ATOM 909 CG LEUA 19117.76218.387 16.8711.00 25.20 A C

ATOM 910 CD7LEUA 19117.10118.593 18.2291.00 23.53 A C

ATOM 911 CD2LEUA 19117.29819.453 15.8551.00 22.75 A C

ATOM 912 C LEUA 19119.56616.070 17.7651.00 26.33 A C

ATOM 913 O LEUA 19118.71115.532 18.4731.00 26.50 A O

ATOM 914 N ALAA 19220.17815.438 16.7601.00 25.06 A N

ATOM 915 CA ALAA 19219.86514.051 16.4381.00 25.25 A C

ATOM 916 CB ALAA 19220.51313.643 15.1151.00 22.30 A C

ATOM 917 C ALAA 19220.30013.079 17.5431.00 27.53 A C

ATOM 918 O ALAA 19219.57812.116 17,8461.00 28.13 A O

ATOM 919 N ALAA 19321.47513.309 18.1351.00 26.81 A N

ATOM 920 CA ALAA 19321.94712.403 19.1781.00 27.54 A C

ATOM 921 CB ALAA 19323.36912.777 19.6161.00 26.31 A C

ATOM 922 C ALAA 19320.98512.459 20.3701.00 27.28 A C

ATOM 923 O ALAA 19320.57511.427 20.9061.00 27,24 A O

ATOM 924 N ILEA 194' 20.62513.672 20.7711.0D 26.82 A N

ATOM 925 CA ILEA 19419.71713.863 21.8831.00 26.83 A C

ATOM 926 CB ILEA 19419.67415.353 22.2641.00 26.75 A C

ATOM 927 CG2ILEA 99418.62515.611 23.3571.00 24.96 A C

ATOM 928 CG1ILEA 19421.07315.761 22.7481.00 27.47 A C

ATOM 929 CD1ILEA 19421.21417.189 23,1371.00 25.31 A C

ATOM 930 C ILEA 19418.31413.336 21.5621.00 28.25 A C

ATOM 931 O ILEA 19417.74612.562 22.3321.00 29.30 A O

ATOM 932 N PHEA 19517.76413.719 20.4151.00 28.54 A N

ATOM 933 CA PHEA 19516.42213.266 20.0591.00 28.12 A C

ATOM 934 CB PHEA 19515.98913.862 18.7151.00 25.79 A C

ATOM 935 CG PHEA 19514.61013.457 18.2901.00 24.25 A C

ATOM 936 CD1PHEA 19513.48813.946 18.9571.00 24.25 A C

ATOM 937 CD2PHEA 19514.42712.566 17.2351.00 23.69 A C

ATOM 938 CE1PHEA 19512.21613.557 18.5901.00 19.79 A C

ATOM 939 CE2PHEA 19513.15112.176 16.8631.00 23.35 A C

ATOM 940 CZ PHEA 19512.04212.677 17.5491:00 21.56 A C

ATOM 941 C PHEA 19516.36011.743 20.0061.00 27,19 A C

ATOM 942 O PHEA 19515.43311.138 20.5351.00 2$.25 A 0 ATOM 943 N ALAA 19617.35111.128 19,3711.00 27.17 A N

ATOM 944 CA ALAA 19617.4039.672 19.2571.00 26.82 A C

ATOM 945 CB ALAA 19618.6429.248 18.4601.00 24.42 A C

ATOM 946 C ALAA 19617.4129.030 20.6541.00 27.54 A C

ATOM 947 O ALAA 19616.7368.030 20.8891.00 26.41 A 0 ATOM 94$ N SERA 19718.1699.624 21.5731.00 27.59 A N

ATOM 949 CA SERA 19718.2439.136 22.9461.00 29.23 A C

ATOM 950 CB SERA 19719.19910.008 23.7621.00 29.33 A C

ATOM 951 OG SERA 19720.5309.892 23.3001.00 31.44 A O

ATOM 952 C SERA 19716.8579.160 23.6071.00 28.86 A C
ATOM 953 O SERA 19716.4538.198 24.2551.00 28.30 A O

ATOM 954 N ALAA 19816.13610.262 23.4201.00 29.16 A N

ATOM 955 CA ALAA 19814.80710.436 24.0061.00 28.77 A C
ATOM 956 CB ALAA 19814.31011.$58 23.7491.00 29.09 A C
ATOM 957 C ALAA 19813.7529.427 23.5411.00 25.37 A C
ATOM 958 O ALAA 19812.9119.014 24,3341.00 26.44 A O
ATOM 959 N ILEA 19913.8059.025 22.2711.00 27.96 A N
ATOM 960 CA ILEA 19912.8248.078 21.7181.00 27.03 A C
ATOM 961 CB ILEA 19912.3908.474 20.2771.00 27.45 A C
ATOM 962 CG2ILEA 19911.8599.907 20.2401.00 26.51 A C
ATOM 963 CG1ILEA 19913.5908.326 19.3281.00 27.74 A C
ATOM 964 CD1ILEA 19913.2338.310 17.8551.00 28.67 A C
ATOM 965 C ILEA 19913.3396.640 21.6011.00 26.83 A C
ATOM 966 O ILEA 19912.5685.742 21.2701.00 25.96 A O
ATOM 967 N HISA 20014.6206.421 21.8851.00 27.56 A N
ATOM 968 CA HISA 20015.2345.099 21.7071.00 27.29 A C
ATOM 969 CB HISA 20016.7075.124 22.1711.00 29.85 A C
ATOM 970 CG HISA 20016.9384.602 23.5601.00 31.89 A C
ATOM 971 CD2HISA 20017.3093.373 23.9961.00 32.99 A C
ATOM 972 ND1HISA 20D16.8165.356 24.6861.00 31.81 A N
ATOM 973 CE1HISA 20017.1024.663 25.7581.00 32.74 A C
ATOM 974 C HISA 20014.5233.862 22.2381.00 27.75 A C
ATOM 975 O HISA 20014.6452.807 21.6421.00 27.88 A O
ATOM 976 NE2HISA 20017,4043.438 25.3681.00 34.57 A N
ATOM 977 N ASPA 20113.7763.963 23.3341.00 28.44 A N
ATOM 978 CA ASPA 20113.0662.780 23.8561.00 29.66 A C
ATOM 979 CB ASPA 20113.6292.352 25.2381.00 32.19 A C
ATOM 980 CG ASPA 20114.8431.413 25.1471.00 32.69 A C

ATOM 981 C ASPA 20111.552 3.009 24.009 1.00 29.11 A C

ATOM 982 0 ASPA 20110.866 2_.20424.646 1.00 27.46 A O

ATOM 983 OD1ASPA 20114.857 0._53124.255 1.00 42.02 A O

ATOM 984 OD2ASPA 20115.776 1.534 25.989 1.00 33.66 A O

ATOM 985 N VALA 20211.024 4.087 23.425 1.00 28.39 A N

ATOM 986 CA VALA 2029.604 4.409 23.589 1.0_028.21 A C

ATOM 987 CB VALA 2029.214 5.706 22.820 1.00 28.53 A C

ATOM 988 CGtVALA 2029.092 5.436 21.342 1.00 27.57 A C

ATOM 989 CG2VALA 2027.919 6.259 23.375 1.00 26.72 A C

ATOM 990 C VALA 2028.633 3.289 23.220 1.00 27,57 A C

ATOM 991 O VALA 2028.788 2.622 22.200 1.00 26.06 A O

ATOM 992 N ASPA 2037.629 3.105 24.078 1.00 27.90 A N

ATOM 993 CA ASPA 2036.601 2.073 23.929 1.00 27.37 A C

ATOM 994 CB ASPA 2035.881 2.225 22,582 1.00 27.02 A C

ATOM 995 CG ASPA 2034,529 1.506 22.547 1.00 28.40 A C

ATOM 996 OD1ASPA 2033.751 1.623 23.520 1.00 27.26 A O

ATOM 997 OD2ASPA 2034.232 0.832 21.535 1.00 27.91 A O

ATOM 998 C ASPA 2037.198 0.658 24.081 1.00 27.64 A C

ATOM 999 O ASPA 2036.775 -0.28723.433 1.00 26.05 A O

ATOM 1000N HISA 2048.205 0.529 24.936 1.00 29.11 A N

ATOM 1001CA HISA 2048.818 -0.77325.186 1.00 30.64 A C

ATOM 1002CB HISA 20410.096 -0.58925.995 1.00 29.70 A C
-ATOM 1003CG HISA 20411.040 -1.74325.888 1.00 31.54 A C

ATOM 1004CD2HISA 20412.326 -1.80525.473 1.00 30.64 A C

ATOM 1005ND1HISA 20410.66fi-3.03826.178 1.00 31.87 A N
i ATOM 1006CEtHISA 20411.681 -3.84825.939 1.00 32.10 A C
' ATOM 1007NE2HISA 20412.700 3.125 25.509 1.00 32.85 A N

ATOM 1008C HISA 2047.799 -1.61525.987 1.00 31.69 A C

ATOM 1009O HISA 2047.268 -1.16127.012 1.00 31:81 A O

ATOM 1010N PROA 2057.501 -2.841_ 25.5261.0D 32.35 A N

ATOM 1011CD PROA 2057.919 -3.46524.251 1.00 32,63 A C

ATOM 1012CA PROA 2056:537 -3.69626.226 1.00 33.27 A C

ATOM 1013CB PROA 2056.084 -4.65625.127 1.00 31.55 A C

ATOM 1014CG PROA 2057.353 -X1:87124,362 1.00 30.71 A C

ATOM 1015C PROA 2057.069 -4.43627.467 1.00 34.71 A C

ATOM 1016O PROA 2056.320 5.156 28.137 1.0D 35.77 A O

ATOM 1017N GLYA 2068.349 -4.26627.777 1.00 34.92 A N

ATOM 1018CA GLYA 2068.901 -4.94128.939 1.00 36.43 A C

ATOM 1019C GLYA 2069.575 -6.27728.658 1.00 37.88 A C

ATOM 1020O GLYA 20610.159 -6.866_2_9.5681.00 39.43 A O

ATOM 1021N VALA 2079.497 -6.75727.414 1.00 37.65 A N

ATOM 1022CA VALA 20710.115 -8.02627.017 1.00 36.79 A C

ATOM 1023CB VALA 2079.051 -9.07326,659 1.0D 36.85 A C

ATOM 1024CG1VALA 2078.339 -9.52627,913 1.00 37.82 A C

ATOM 1025CG2VALA 2078.056 -8.49425.678 1.00 37.82 A C

ATOM 1026C VALA 20711.069 -7.85125.831 1.00 36.38 A C

ATOM 1027O VALA 20711.025 -6.83825.141 1.00 37.33 A O
ATOM 1028N SERA 20811.916 -8.84125.576 1.00 35,16 A N

ATOM 1029CA SERA 20812.896 -8.73024.490 1.00 34.92 A C
ATOM 1030CB SERA 20814.111 -9.60824.800 1.00 32.07 A C

ATOM 1031OG SERA 20813.767 -10.97524.685 1.00 33.26 A O

ATOM 1032C SERA 20812.425 -9.04523.064 1.00 34.37 A C

ATOM 1033O SERA 20811.303 -9.50122.826 1.00 33.04 A O

ATOM 1034N ASNA 20913.312 -8.79122.110 1.00 35.38 A N
ATOM 1035CA ASNA 20913.005 -9.06920.717 1.00 36.69 A C

ATOM 1036CB ASNA 20914.187 -8.71219.811 1.00 35.48 A C

ATOM 1037CG ASNA 20914.217 -7.23819.445 1.00 35.53 A C
ATOM 1038ODtASNA 20913,169 -6.60219.313 1.00 36.37 A O

ATOM 1039ND2ASNA 20915.411 -6.69719.254 1.00 33.12 A N
ATOM 1040C ASNA 20912.688 -10.54020.561 1.00 38.00 A C

ATOM 1041O ASNA 20911.673 -10.91619.960 1.00 38.79 A O
ATOM 1042N GLNA 21013.560 -11.37121.119 1.00 39.18 A N
ATOM 1043CA GLNA 21013.393 -12.81021.020 1.00 40.51 A C

ATOM 1044CB GLNA 21014.465 -13.52421.835 1.00 42.91 A C
ATOM 1045CG GLNA 21014.669 -14.94021.385 1.00 45.77 A C
ATOM 1046CD GLNA 21015.158 -15.00019.960 1.00 47.26 A C
ATOM 1047OE1GLNA 21016.289 -14.60619.672 1.00 49,75 A O

ATOM 1048NE2GLNA 21014.308 -15.47819,051 1.00 46.32 A N
ATOM 1049C GLNA 21012.015 -13.25121.493 1.00 39.61 A C

ATOM 1050O GLNA 21011,377 -14.09720,872 1.00 38.88 A O

ATOM 1051N PHEA 21111.556 -12.66522.591 1.00 38.68 A N
ATOM 1052GA PHEA 21110.261 -13.01823.130 1.00 38.73 A C

ATOM 1053CB PHEA 21110.056 -12.31824.477 1.00 39.63 A C
ATOM 1054CG PHEA 2118.740 -12.63325.131 1.00 41.62 A C

ATOM 1055CD1PHEA 2117.622 -11.84224.891 1.00 42.76 A C

ATOM 1056CD2PHEA 2118.616 -13.73125.979 1.00 43.53 A C

ATOM 1057CE1PHEA 2116.392 -12.13525.490 1.00 43.75 A C

ATOM 1058CE2PHEA 2117.391 -14.03826.584 1.00 43.85 A C
ATOM 1059CZ PHEA 2116.277 -13.23526.337 1.00 44,02 A C

ATOM 1060C PHEA 2119.127 -12.68122,160 1.00 38.87 A C
ATOM 1061O PHEA 2118.235 -13.50421.934 1.00 38.43 A O
ATOM 1062N LEUA 2129.159 -11.47921.584 1.00 38.13 A N

ATOM 1063CA LEUA 2128.120 -11.05920.639 1.0D 37.52 A C
ATOM 1064CB LEUA 2125.337 -9.60020.227 1.00 36.72 A C

ATOM 1065CG LEUA 2128.240 -8.56221.350 1.00 36.60 A C
ATOM 1066CD1LEUA 2128.659 -7.19120.841 1.00 36.90 A C

ATOM 1067CD2LEUl 2126.807 -8.53521.8821.00 __ A C
A 35.73 ATOM 1068C LEUA 2128.137 -11.95619.4041.00 38.29 A C

ATOM 1069O LEUA 2127.096 -12.23918.8071.00 38.50 A 0 ATOM 1070N ILEA 2139.331 -12.40219.0321.00 39.01 A N

ATOM 1071CA ILEA 2139.506 -13.27217.8781.00 40.65 A C

ATOM 1072CB ILEA 21311.007 -13.40117.5271.00 39.67 A C

ATOM 1073CG2ILEA 21311.207 -14.44616.4351.00 39.27 A C

ATOM 1074CG7ILEA 21311.558 -12.03117.1071.00 39.78 A C

ATOM 1075CD1ILEA 21313.057 -12.00616.8251.00 36.47 A C

ATOM 1076C ILEA 2138.933 -14.67518.1281.00 42.82 A C

ATOM 1077O ILEA 2138.108 -15.17517.3581.00 42.42 A O

ATOM 1078N ASNA 2149.364 -15.30719.2141.00 44.70 A N

ATOM 1079CA ASNA 2148.902 -16.65219.5191.00 46.67 A C

ATOM 1080CB ASNA 2149.726 -17.24920.6671.00 46.78 A C

ATOM 1081CG ASNA 21411.222 -17.27020.3641.00 47.42 A C

ATOM 1082OD1ASN~ 21411.638 -17.26119.2011.00 45.80 A O
A

ATOM 1083ND2ASNA 21412.037 -17.30921.4151.D0 48.17 A N

ATOM 1084C ASNA 2147.413 -16.72919.8451.00 47.39 A C

ATOM 1085O ASNA 2146.814 -17.79719.7521.00 48.54 A O

ATOM 1086N THRA 2156.815 -15.60320.2161.00 47.01 A N

ATOM 1087CA THRA 2955.396 -15.58520.5481.00 46.98 A C

ATOM 1088CB THRA 2155.091 -14.58321.6971.00 46.74 A C

ATOM 1089OG1THRA 2155.706 -13.31921.4151.00 45.74 A O

ATOM 1090CG2THRA 2155.610 -15.11723.0261.00 45.89 A C

ATOM 1091C THRA 2154.521 -15.22419.3561.00 47.43 A C

ATOM 1092O THRA 2153.295 -15.28699.4441.00 47.74 A O

ATOM 1093N ASNA 2165.152 -14.83818.2481.00 48.16 A N

ATOM 1094CA ASNA 2164.424 -14.45217.0421,00 48.08 A C

ATOM 1095CB ASNA 2163.427 -15.54216.6471.00 50.45 A C

ATOM 1096CG ASNA 2163.995 -16.50915.6501.00 52.17 A C

ATOM 1097OD1ASNA 2164.333 -16.12814.5281.00 54.91 A O

ATOM 1098ND2ASNA 2164.108 -17,77316.0441.00 53.79 A N

ATOM 1099C ASNA 2163.671 -13.13417.1951.00 47.25 A C

ATOM 1100O ASNA 2162.559 -12.99016.6691.00 47.22 A O

ATOM 1101N SERA 2174.265 -12.18017.9111.00 45.44 A N

ATOM 1102CA SERA 2173.629 -10.87718.1171.00 44.18 A C

ATOM 1103CB SERA 2174.486 -9.99919.0241.00 43.87 A C

ATOM 1104OG SERA 2175.700 -9.65718.3841.00 43.03 A O

ATOM 1105C SERA 2173.457 -10.17916.7751.00 43.82 A C

ATOM 1106O SERA 2174.246 -10.40615.8521.00 43.18 A O

ATOM 1107N GLUA 2182.437 -9.33216.6561.00 43.59 A N

ATOM 1108CA GLUA 2182.228 -8.63315.3961.00 44.64 A C

ATOM 1109CB GLUA 2180.935 -7.80515.4161.00 45.80 A C

ATOM 1110CG GLUA 2180.978 -6.57516.2831.00 48.18 A C

ATOM 1111CD GLUA 218-0.160 -5.59915.9951.00 50.23 A C

ATOM 1112OE1GLUA 218-0.249 -4.57716.7241.00 51.43 A O

ATOM 1113OE2GLUA 218-0.949 -5.84015.0481.00 48.18 A O

ATOM 1114C GLUA 2183.431 -7.73215.1101.00 43.77 A C

ATOM 1115O GLUA 2183.822 -7.54713.9571.00 42.97 A 0 ATOM 1116N LEUA 2194.019 -7.19216.1731.00 42.5 A N

ATOM 1117CA LEUA 2195.178 -6.32216.0631.00 _ A C

.31 ATOM 1118CB LEUA 2195.654 -5.93317.4621.00 _ A C
40.94 ATOM 1119CG LEUA 2196.048 -4.47917.7171.00 40.60 A C

ATOM 1120CD1LEUA 2195.172 -3.51816.8991.00 39.37 A C

ATOM 1121CD2LEUA 2195.917 -4.19919.2111.00 _ A C
39.54 ATOM 1122C LEUA 2196.296 -7.03115.3041.00 43.30 A C

ATOM 1123O LEUA 2196.896 -6.46014.3891.00 44.1 A O

ATOM 1124N ALAA 2206.563 -8.27815.6801.00 _ A N
43.38 ATOM 1125CA ALAA 2207.604 -9.08215.0411.00 44.16 A C

ATOM 1126CB ALAA _2207.776 -10.39915.7861.00 43.95 A C

ATOM 1127C ALAA 2207.295 -9.36513.5711.00 45.06 A C

ATOM 1128O ALAA 220__8.192 -9.34212.7191.00 _ A 0 44.59 ATOM 1129N LEUA 2216.026 -9.64013.2801.00 45.61 A N

ATOM 1130CA LEUA 2215.602 -9.93711.9201.00 46.01 A C

ATOM 1131CB LEUA 221_4.162 -10.47211.9181.00 47.49 A C

ATOM 1132CG LEUA 2213.849 -11.62512.8991.00 50.28 A C

ATOM 1133CD1LEUA 2212.3_98 -12.09512.7001.00 49.74 A C

ATOM 1134CD2LEUA 2214.820 -12.79612.6911.00 48.97 A C

ATOM 1135C LEUA 2215.715 -8.68111.0591.00 45.67 A C

ATOM 1136O LEUA 2216.149 -8.7449.909 1.00 45.95 A O

ATOM 1137N META 2225.344 -7.54111.6281.00 44.82 A N

ATOM 1138CA META 2225.410 -6.27010.9171.00 45.01 A C

ATOM 1139CB META 2224.852 -5.15011.8071.00 46.22 A C

ATOM 1140CG META 2225.039 -3.72111.2991.00 48.99 A C

ATOM 1141SD META 2224.194 -3.2829.749 1.00 54.02 A S

ATOM 1142CE META 2222.424 -3.48610.2141.00 53.30 A C

ATOM 1143C META 2226.859 -5.97610.5141.00 43.45 A C

ATOM 1144O META 2227.131 -5.62 9.358 1.00 43.02 A O

ATOM 1145N TYRA 2237.782 _ 11.4571.00 40.70 A N
-6.161 ATOM 1146CA TYRA 2239.201 -5.9101 1.00 39.39 A C
1.209 ATOM 1147CB TYRA 2239.813 -5.207_ 1.00 36.02 A C
12.430 ATOM 1148CG TYRA 2239.263 -3.80212.5831.00 34.90 A C

ATOM 1149CD1TYRA 2239.513 -2.83611.6071.00 33.27 A C

ATOM 1150CE1TYRA 2238.952 -1.57511.6771.00 31.74 A C

ATOM 1151CD2TYRA 2238.430 3.460 13.6431.00 32.73 A C

I 1152CE2TYRA 2237:855 -2 13 1 00 32 A C
ATOM ~ ~ ~ ~ ~ ~ 190 721 96 ~

ATOM1153CZ TYRA 2238.125_ -1.25112.728 1.00 32.68 A C

ATOM1154OH TYRA 2237.578 0.013 12.780 1.00 31.03 A 0 ATOM1155C TYRA 22310.010 -7.14910.815 1.00 39.41 A C

ATOM1156O TYRA 22311.231 -7.18410.936 1.00 39.34 A O

ATOM1157N ASNA 2249.3_11 -8.16210.324 1.00 40.43 A N

ATOM1158CA ASNA 2249.951 -9.3979.883 1.00 41.10 A C

ATOM1159CB ASNA 22410.482 -9.1998.462 1.00 39.99 A C

ATOM1160CG ASNA 2249.400 -8.7417.507 1.00 40.26 A C

ATOM1161OD1ASNA 2248.38_9_-9.4197.333 1.00 41.69 A 0 ATOM1162ND2ASNA 2249:597 -7.5816.893 1.00 40.24 A N

ATOM1163C ASNA 22411.063 -9.87610.816 1.00 41.22 A C

ATOM1164O ASNA 22412.174 -10.18610.376 1.00 41.66 A O

ATOM1165N ASPA 22510.741 -9.92712.109 1.00 41.49 A N

ATOM1166CA ASPA 22511.655 -10.38013.162 1.00 40.67 A C

ATOM1167CB ASPA 22511.862 -11.89113.074 1.00 40.84 A C

ATOM1168CG ASPA 22510.567 -12.65813.066 1.00 42.41 A C

ATOM1169OD1ASPA 2259.603 -12.22013.729 1.00 43.88 A O

ATOM1170OD2ASPA 22510.515 -13.71312.403 1.00 43.43 A O

ATOM1171C ASPA 22513.030 -9.72613.213 1.00 40.11 A C

ATOM1172O ASPA 22513.933 -10.25413.867 1.00 40.27 A 0 ATOM1173N SERA 22613.203 -8.58812.551_1.00 39.12 A N

ATOM1174CA SERA 22614.514 -7.92412.548 1.00 38.65 A C

ATOM1175CB SERA 22614.962 -7.64611.111 1.00 39.07 A C

ATOM1176OG SERA 22614.710 -8.76710.290 1.00 42.50 A O
~

ATOM1177C SERA 22614.478 -6.61513.315 1.00 36.13 A C

ATOM1178O SERA 22613.717 -5.71812.965 1.00 35.94 A O

ATOM1179N SERA 22715.315 -6.50514.344 1.00 34.31 A N

ATOM1180CA SERA 22715.372 -5.30715.179 1.00 32.12 A C

ATOM1181CB SERA 22716.161 -4.21214.473 1.00 32.12 A C

ATOM1182OG SERA 22717.535 -4.52514.416 1.00 31.84 A O

ATOM1183C SERA 22713.958 -4.81315.486 1.00 31.33 A C

ATOM1184O SERA 22713.667 -3.61115.415 1.00 30.64 A O

ATOM1185N VALA 22813.088 -5.76215.815 1.00 30.08 A N

ATOM1186CA VALA 22811.685 -5.48416.113 1.00 28.84 A C

ATOM1187CB VALA 22811.040 -6.69916.781 1.00 27.84 A C

ATOM1188CG1VALA 2289.592 -6.41817.111 1.00 28.86 A C

ATOM1189CG2VALA 22811.173 -7.89515.874 1.00 28.89 A C

ATOM1190C VALA 22811.450 -4.26116.997 1.00 28.46 A C

ATOM1191O VALA 22810.868 -3.27016.565 1.00 27.56 A 0 ATOM1192N LEUA 22911.905 -4.32518.238 1.00 28.33 A N

ATOM1193CA LEUA 22911.690 -3.21419.141 1.00 27,91 A C

ATOM1194CB LEUA 22912.200 -3.56320.539 1.00 28.51 A C

ATOM1195CG LEUA 22911.353 -4.59721.289 1.00 30.46 A C

ATOM1196CD1LEUA 22912.089 5.056 22.522 1.00 30.01 A C

ATOM1197CD2LEUA 2299.997 -3.99721.657 1.00 31.82 A C

ATOM1198C LEUA 22912.318 -1.91518.669 1.00 27.36 A C

ATOM1199O LEUA 22911.677 -0.87518.722 1.00 26.66 A O

ATOM1200N GLUA 23013.565 -1.97018.215 1.00 28.00 A N

ATOM1201CA GLUA 23014.254 -0.76417.769 1.00 28.87 A C

ATOM1202CB GLUA 23015.690 -1.08617.340 1.00 30.19 A C

ATOM1203CG GLUA 23016.638 -1.51918.470 1.00 33.75 A C

ATOM1204CD GLUA 23016.301 -2.87919.064 1.00 34.62 A C

ATOM1205OE1GLUA 23015.724 -3.72518.344 1.00 36.57 A O

ATOM1206OE2GLUA 23016.630 -3.11020.251 1.00 36.80 A O

ATOM1207C GLUA 23013.506 -0.07816.619 1.00 28.75 A C

ATOM1208O GLUA 23013.420 1.155 16.560 1.00 27.57 A O

ATOM1209N ASNA 23112.974 -0.87815.704 1.00 28.14 A N

ATOM1210CA ASNA 23112.237 -0.31914.594 1.00 28.51 A C

ATOM1211CB ASNA 23111,880 -1.40113.571 1.00 29.03 A C

ATOM1212CG ASNA 23112.862 -1.44212.401 1.00 30.46 A C

ATOM1213OD1ASNA 23113.076 -0.43011.725 1.00 29.50 A O

ATOM1214ND2ASNA 23113.462 -2.60912.162 1.00 27.07 A N

ATOM1215C ASNA 23110.973 0.334 15.107 1.00 27.05 A C

ATOM1216O ASNA 23110.588 1.411 14.643 1.00 26.03 A O

ATOM1217N HISA 23210.345 -0.31716.080 1.00 25.15 A N

ATOM1218CA HISA 2329.100 0.177 16.641 1.00 24.96 A C

ATOM1219CB HISA 2328.471 -0.89217.534 1.00 26.35 A C

ATOM1220CG HISA 2327.163 -0.48018.127 1.00 26.87 A C

ATOM1221CD2HISA 2326.726 -0.47519.407 1.00 27.54 A C

ATOM1222ND1HISA 2326.116 -0.01517.364 1.00 27.81 A N

ATOM1223CE1HISA 2325.089 0.255 18.147 1.00 27.62 A C

ATOM1224NE2HISA 2325.433 -0.01519.392 1.00 26.71 A N

ATOM1225C HISA 2329.293 1.469 17.415 1.00 24.46 A C

ATOM1226O HISA 2328.487 2.383 17.297 1.00 25.26 A O

ATOM1227N HISA 23310.365 1.547 15.197 1.00 24.08 A N

ATOM1228CA HISA 23310.663 2.752 18.970 1.00 25.46 A C

ATOM1229CB HISA 23311.987 2.617 19.742 1.00 27.15 A C

ATOM1230CG HISA 23312.044 1.452 20.684 1.00 28.09 A C
ATOM1231CD2HISA 23313.053 0.595 20.974 1.00 27.54 A C
ATOM1232ND1HISA 23310.986 1.087 21.492 1.00 28.02 A N

ATOM1233CE1HISA 23311.342 0.053 22.235 1.00 26.78 A C

ATOM1234NE2HISA 23312.590 -0.26421.941 1.00 27.00 A N

ATOM1235C HISA 23310.793 3.932 18.011 1.00 25.04 A C
ATOM1236O HISA 23310.240 5.006 18.253 1.00 25.57 A O

ATOM1237N LEUA 23411.556 3.738 16.939 1.00 23.30 A N

ATOM1238CA LEUA 23411.732 4.792 15.941 1.00 24.20 A C

ATOM1239CB LEUA 23412.677 4.329 _ 14.8361.00 23.87 A C

ATOM1240CG LEUA 23414.151 4.385 15.109 1.00 25.83 A C

ATOM1241CD1LEUA 23414.876 3.543 14.048 1.00 25.18 A C

ATOM1242CD2LEUA 23414.696 5.822 15.073 1.00 21.25 A C

ATOM1243C LEUA 23410.382 5.157 15.319 1.00 23.50 A C

ATOM1244O LEUA 23410.015 6.318 15.278 1.00 23.27 A O

ATOM1245N ALAA 2359.641 4.160 14.843 1.00 24.19 A N

ATOM1246CA ALAA 2358.349 4.433 14.218 1.00 24.77 A C

ATOM1247CB ALAA 2357.643 3.127 13.841 1.00 21.75 A C

ATOM1248C ALAA 2357.465 5.278 15.134 1.00 25.28 A C

ATOM1249O ALAA 2356.882 6.276 14.701 1.00 26.95 A O

ATOM1250N VALA 2367.388 4.893 16.403 1.00 24.45 A N

ATOM1251CA VALA 2366.592 5.620 17.377 1.00 23.38 A C

ATOM1252CB VALA 2366.510 4.522 18.702 1.00 22.79 A C

ATOM1253CG1VALA 2365.815 5.662 19.783 1.00 19.98 A C

ATOM1254CG2VALA 2365.750 3.501 18.465 1.00 21.14 A C

ATOM1255C VALA 2367.139 7.024 17.672 1.00 25.10 A C

ATOM1256O VALA 2366.378 7.979 17.797 1.00 26.07 A O

ATOM1257N GLYA 2378.455 7.149 17.791 1.00 25.27 A N

ATOM1258CA GLYA 2379.043 8.449 18.084 1.00 26.76 A C

ATOM1259C GLYA 2375.710 9.492 17.035 1.00 27.43 A C

ATOM1260O GLYA 2378.352 10.63117.347 1.00 27.05 A O

ATOM1261N PHEA 2388.831 9.101 15.774 1.00 27.42 A N

ATOM1262CA PHEA 2388.526 10.00914.681 1.00 28.12 A C

ATOM1263CB PHEA 2389.096 9.459 13.383 1.00 27.14 A C

ATOM1264CG PHEA 23810.566 9.612 13.281 1.00 27.65 A C

ATOM1265CD1PHEA 23811.135 10.88013.235 1.00 27.66 A C

ATOM1266CD2PHEA 23811.390 8.500 13.229 1.00 27.77 A C

ATOM1267CE1PHEA 23812.522 11.03913.134 1.00 29.37 A C

ATOM1268CE2PHEA 23812.773 8.645 13.127 1.00 29.10 A C

ATOM1269CZ PHEA 23813:340 9.910 13.080 1.00 27.25 A C

ATOM1270C PHEA 2387.031 10.23014.535 1.00 28.12 A C

ATOM1271O PHEA 2386.578 11.35714.355 1.00 27.55 A O

ATOM1272N LYSA 2396.283 9.135 14.622 1.00 29.06 A N

ATOM1273CA LYSA 2394.831 9.139 14.515 1.00 28.57 A C

ATOM1274CB LYSA 2394.303 7.736 14.806 1.00 31.79 A C

ATOM1275CG LYSA 2392.831 7.571 14.561 1.00 35.54 A C

ATOM1276CD LYSA 2392.525 7.790 13.090 1.00 38.22 A C

ATOM1277CE LYSA 2391.047 7.623 12.799 1.00 40.21 A C

ATOM1278NZ LYSA 2390.796 7.920 11.375 1.00 41.18 A N

ATOM1279C LYSA 2394.177 10.13015.474 1.00 28.10 A C

ATOM12800 LYSA 2393.192 10.77915.132 1.00 28.06 A O

ATOM1281N LEUA 2404.736 10.26416.671 1.00 27.24 A N

ATOM1282CA LEUA 2404.162 11.17117.655 1.00 25.88 A C

ATOM1283CB LEUA 2404.768 10.90619.033 1.00 25.24 A C

ATOM1284CG LEUA 2404.476 9.523 19.628 1_.00 25.73 A C

ATOM1285CD1LEUA 2405.065 9.459 21.035 1.00 25.94 A C

ATOM1286CD2LEUA 2402.965 9.254 19.668 1.00 25.83 A C

ATOM1287C LEUA 2404.280 12.65017.310 1.00 26.26 A C

ATOM1288O LEUA 2403.586 13.48217.915 1.00 24.82 A O

ATOM1289N LEUA 2415.162 12.97416.358 1.00 24.54 A N

ATOM1290CA LEUA 2415.362 14.34615:906 1.00 25.24 A C

ATOM1291CB LEUA 2416.522 14.41414.896 1.0D 25.85 A C

ATOM1292CG LEUA 2417.947 14.11415.365 1.00 24.24 A C

ATOM1293CD1LEUA 2418.824 13.77314.135 1.00 21.74 A C

ATOM1294CD2LEUA 2418.479 15.31316.141 1.00 19.53 A C

ATOM1295C LEUA 2414.083 14.85515.214 1.00 25.63 A C

ATOM12960 LEUA 2413.845 16.05615.106 1.00 24.53 A O

ATOM1297N GLNA 2423.273 13.91814.745 1.00 26.36 A N

ATOM1298CA GLNA 2422.037 14.23614.056 1.00 28.31 A C

ATOM1299CB GLNA 2421.655 13.08413.135 1.00 29.69 A C

ATOM1300CG GLNA 2422.585 12.86311.959 1.00 33.13 A C

ATOM1301CD GLNA 2422.246 11.57811.253 1.00 38.09 A C

ATOM1302OE1GLNA 2421.126 11.07711.386 1.00 41.59 A O

ATOM1303NE2GLNA 2423.196 11:03210.494 1.00 40.84 A N

ATOM1304C GLNA 2420.838 14.56114.935 1.00 28.81 A C

ATOM1305O GLNA 242-0.197 14.94714.413 1.00 30.21 A O

ATOM1306N GLUA 2430.937 14.39916.249 1.00 26.78 A N

ATOM1307CA GLUA 243-0.226 14.71117.074 1.00 28.56 A C

ATOM1308CB GLUA 243-0.146 14.02018.449 1.00 27.34 A C

ATOM1309CG GLUA 243-0.115 12.49518.358 1.00 27.47 A C

ATOM1310CD GLUA 243-0.629 11.77719.627 1.00 29.24 A C

ATOM1311OE1GLUA 243-0.728 12.42920.693 1.00 28.17 A O

ATOM1312OE2GLUA 243-0.927 10.55319.553 1.00 26.60 A O

ATOM1313C GLUA 243-0.366 16.22317.217 1.00 28.89 A C

ATOM1314O GLUA 2430.569 16.96816.930 1.00 30.24 A O

ATOM1315N GLUA 244-1.536 16.67517.659 1.00 29.54 A N

ATOM1316CA GLUA 244-1.802 18.09917.784 1.00 28.44 A C

ATOM1317CB GLUA 244-3.105 18.32818.559 1.00 28.69 A C

ATOM1318CG GLUA 244-3.672 19.75018.473 1.00 28.84 A C

ATOM1319CD GLUA 244-3.953 20.20917.042 1.00 26.61 A C

ATOM1320OE1GLUA 244-4.235 19.37916.167 1.00 26.36 A O

ATOM1321OE2GLUA 244-3.900 21.41716.787 1.00 28.72 A O

ATOM1322C GLUA 244-0.647 18.84018.449 1.00 29.55 A C

ATOM1323O GLUA 244-0.174 18.45619.531 1.00 29.14 A O

ATOM1324N ASNA 245-0.200 19.89917.772 1.00 28.52 A N

ATOM1325CA ASNA 2450.897 20.75418_229 1.00 27.31 A C

ATOM1326CB ASNA 2450.411 21.65819.374 1.00 27.50 A.C

ATOM1327CG ASNA 2451.333 22.83019.621 1.00 28.74 A C

ATOM1328OD1ASNA 2451.339 23.41020.707 1.00 32.85 A O

ATOM1329ND2ASNA 2452.118 23.18718.617 1.00 28.69 A N

ATOM1330C ASNA 2452.116 19.93918.685 1.00 25.19 A C

ATOM1331O ASNA 2452.738 20.24119.697 1.00 25.37 A 0 ATOM1332N CYSA 2462.466 18.90317.943 1.00 25.38 A N

ATOM1333CA CYSA 2463.622 18.11418.332 1.00 26.77 A C

ATOM1334CB CYSA 2463.205 16.66018.583 1.00 27.55 A C

ATOM1335SG CYSA 2462.318 16.40420.127 1.00 24.31 A S

ATOM1336C CYSA 2464.805 18.12517.368 1.00 27.32 A C

ATOM1337O CYSA 2465.840 17.54617.687 1.00 28.18 A O

ATOM1338N ASPA 2474.694 18.77116.209 1.00 26.02 A N

ATOM1339CA ASPA 2475.834 18.72815.274 1.00 26.69 A C

ATOM1340CB ASPA 2475.374 18.88513.819 1.00 24.48 A C

ATOM1341CG ASPA 2476.521 18.71212.834 1.00 27.08 A C

ATOM1342ODtASPA 2477.620 18.26613.272 1.00 22.20 A O

ATOM1343OD2ASPA 2476.324 19.01111.627 1.00 25.43 A O

ATOM1344C ASPA 2476.931 19.74415.577 1.00 26.14 A C

ATOM1345O ASPA 2476.946 20.84315.021 1.00 25.81 A O

ATOM1346N ILEA 2487.845 19.34916.462 1.00 25.95 A N

ATOM1347CA ILEA 2488.941 20.19916.898 1.00 26.16 A C

ATOM1348CB ILEA 2489.706 19.56618.084 1.00 26.14 A C

ATOM1349CG2ILEA 2488.790 19.46319.319 1.00 24.71 A C

ATOM1350CG1ILEA 24810.244 18.19717.683 1.00 25.27 A C

ATOM1351CD1ILEA 24811.193 17.60818.706 1.00 26.35 A C
' ATOM1352C ILEA 2489.939 20.51515,787 1.00 27.14 A C
;

ATOM1353O ILEA 24810.792 21.38615.956 1.00 28.15 A O

ATOM1354N PHEA 2499.831 19.80614.661 1.00 25.94 A N

ATOM1355CA PHEA 24910.707 20.03013.517 1.00 25.50 A C

ATOM1356CB PHEA 24911.234 18.68912.986 1.00 24.77 A C

ATOM1357CG PHEA 24911.899 17.82414.043 1.00 25.97 A C

ATOM1358CD1PHEA 24912.854 18.35414.903 1.00 26.30 A C

ATOM1359CD2PHEA 24911.581 16.47814.158 1.00 26.45 A C

ATOM1360CE1PHEA 24913.485 17.56415.862 1.00 26.95 A C

ATOM1361CE2PHEA 24912.212 15.67415.118 1.00 29.14 A C

ATOM1362CZ PHEA 24913.167 16.22415.972 1.00 27.11 A C

ATOM1363C PHEA 2499.977 20.78612.380 1.00 26.67 A C

ATOM1364O PHEA 24910.481 20.86911.261 1.00 27.25 A O

ATOM1365N GLNA 2508.801 21.34812.666 1.00 26.30 A N

ATOM1366CA GLNA 2508.028 22.05511.636 1.00 26.47 A C

ATOM1367CB GLNA 2506.775 22.67912.250 1.00 25.33 A C

ATOM1365CG GLNA 2507.033 23.58413.418 1.00 27.69 A C

ATOM1369CD GLNA 2505.756 23.90614.163 1.00 31.32 A C

ATOM1370OE1GLNA 2505.114 23.02014.742 1.00 30.52 A O

ATOM1371NE2GLNA 2505.371 25:17314.144 1.00 32.01 A N

ATOM1372C GLNA 2508.816 23.11910.873 1.00 25.68 A C

ATOM1373O GLNA 2508.600 23.3149.688 1.00 23.11 A O

ATOM1374N ASNA 2519.750 23.77911.549 1.00 27.27 A N

ATOM1375CA ASNA 25110.549 24.81510.918 1_.00 28.66 A C

ATOM1376CB ASNA 25110.750 25.96911.888 1.00 29.14 A C

ATOM1377CG ASNA 2519.477 26.71912.121 1.00 29.60 A C

ATOM1378ODtASNA 2518.721 26.94011.180 1.00 31.67 A O

ATOM1379ND2ASNA 2519.224 27.11813.360 1.00 28.45 A N

ATOM1380C ASNA 25111.886 24.41510.314 1.00 29.88 A C

ATOM1381O ASNA 25112.616 25.2649.840 1.00 31.11 A 0 ATOM1382N LEUA 25212.224 23.13610.337 1.00 30.74 A N

ATOM1383CA LEUA 25213.475 22.7089.723 1.0D 31.26 A C

ATOM1384CB LEUA 25213.936 21.35310.287 1.00 30.24 A C
.

ATOM1385CG LEUA 25214.805 21.29711.547 1.00 31.16 A C

ATOM1386CD1LEUA 25214.122 22.01312.700 1.0D 30.34 A C

ATOM1387CD2LEUA 25215.076 19.83011.901 1.00 30.08 A C

ATOM1388C LEUA 25213.189 22.5528.229 1.00 31.93 A C

ATOM13890 LEUA 25212.098 22.1157.852 1.00 32.63 A O

ATOM1390N THRA 25314.152 22.9107.381 1.00 30.79 A N

ATOM1391CA THRA 25313.968 22.7625.940 1.00 29.21 A C

ATOM1392CB THRA 25315.154 23.3665.146 1.00 30.08 A C

ATOM1393OG1THRA 25316.321 22.5575.350 1.00 29.64 A O

ATOM1394CG2THRA 25315.448 24.7875.605 1.00 29.22 A C

ATOM1395C THRA 25313.946 21.2625.653 1.00 28.13 A C

ATOM13960 THRA 25314.381 20.4716.480 1.00 29.14 A O

ATOM1397N LYSA 25413.460 20.8734.485 1.00 26.87 A N

ATOM1398CA LYSA 25413.429 19.4604.112 1.00 28.00 A C

ATOM1399CB LYSA 25412.864 19.2932.700 1.00 25.99 A C

ATOM1400CG LYSA 25412.863 17.8602.201 1.00 27.11 A C

ATOM1401CD LYSA 25411.834 17.0152.933 1.00 28.89 A C

ATOM1402CE LYSA 25411.729 15.6112.315 1.00 29.91 A C

ATOM1403NZ LYSA 25410.563 14.8452.866 1.00 25.67 A N

ATOM1404C LYSA 25414.818 18.8044.172 1.00 28.57 A C

ATOM1405O LYSA 25414.937 17.6184.498 1.00 27.40 A O

ATOM1406N LYSA 25515.860 19.5663.836 1.00 29.49 A N

ATOM1407CA LYSA 25517.221 19.0443.875 1.00 30.18 A C

ATOM1408CB LYSA 25518.229 20.0403.295 1.00 33.00 A C

ATOM1409CG LYSA 25518.469 19.8851.811 1.00 35.16 A C

ATOM1410CD LYSA 25519.631 20.7671.355 1.00 41.50 A C

ATOM 1411CE LYSA 25519.820 20.707-0.163 1.00 43.10A C

ATOM 1412NZ LYSA 25520.031 19.297-0.643 1,00 44.74A N
ATOM 1413C LYSA 25517.598 18.7315.301 1.00 28.44A C

ATOM 1414O LYSA 25518.077 17.6515.578 1.00 28.79A O

ATOM 1415N GLNA 25617.383 19.6786.208 1,00 29.47A N

ATOM 1416CA GLNA 25617.692 19.4557.620 1.00 28.52A C

ATOM 1417CB GLNA 25617.341 20.6858.462 1,00 28.48A C

ATOM 1418CG GLNA 25618.292 21.8768.3_06 1.00 27.78A C

ATOM 1419CD GLNA 25617.824 23.1019.089 1,00 28.79A C

ATOM 1420OE1GLNA 25616.711 23.585_ 1.00 29.93A O
8.891 ATOM 1421NE2GLNA 25618.677 23.6129.969 1.00 29.19A N

ATOM 1422C GLNA 25616.925 18.2488.153 1.00 29.21A C

ATOM 1423O GLNA 25617.471 17,4478.903 1.00 29.98A O

ATOM 1424N ARGA 25715.664 18.1127.755 1.00 28.88A N

ATOM 1425CA ARGA 25714.832 _17.0018.222 1.00 28.86A C

ATOM 1426CB ARGA 25713.358 17.2537.872 1.00 27.12A C

ATOM 1427CG ARGA 25712.742 18.4048.667 1.00 25.66A C

ATOM 1428CD ARGA 25711.257 18.604_ 1.00 26.65A C
8.375 ATOM 1429NE ARGA 25710.970 19.3867,168 1,00 27.49A N

ATOM 1430CZ ARGA 25T10.370 18.8986.080 1.00 28.34A C

ATOM 1431NHtARGA 25710.003 17.6266,034 1.00 29,97A N

ATOM 1432NH2ARGA 25710.095 _19.6875.052 1,00 28.05A N
ATOM 1433C ARGA 25715.274 15.6497.674 1,00 29.36A C
ATOM 1434O ARGA 25715.271 14.6478.394 1.00 29.59A O

ATOM 1435N GLNA 25815.655 15.6046.404 1.00 29.66A N

ATOM 1436CA GLNI 25816.104 14.3445.850 1.00 30.80A C
A

ATOM 1437CB GLNA 25816.231 14.4244.333 1.00 30.63A C

ATOM 1438CG GLNA 25814.887 14.2663.656 1.00 33.54A C

ATOM 1439CD GLNA 25815.005 13.9882,180 1.00 34.65A C

ATOM 1440OE1GLNA 25814.322 13.1061.645 1.00 35.61A O

ATOM 1441NE2GLNA 25815.868 14.7361.508 1.00 32.17A N

ATOM 1442C GLNA 25817.419 13.9206.489 1.00 30:60A C

ATOM 1443O GLNA 25817.635 12.7386.722 1.00 29.68A O

ATOM 1444N SERA 25918.283 14,8816.796 1.00 30.59A N

ATOM 1445CA SERA 25919.559 14.5547.432 1.00 32.21A C

ATOM 1446CB SERA 25920.495 15.7677.393 1.00 33.60A C

ATOM 1447OG SERA 25921.725 15.4828.035 1.0D 36.77A O

ATOM 1448C SERA 25919.325 14.1128.887 1.00 32.10A C

ATOM 1449O SERA 25919.798 13.0529.319 1.00 33.52A O

ATOM 1450N LEUA 26018.588 14,9299.630 1.00 29.36A N

ATOM 1451CA LEUA 26018.261 14.63411.018 1.00 28.86A C

ATOM 1452CB LEUA 26017.221 15.63511.535 1.00 26.07A C

ATOM 1453CG LEUA 26016.730 15.49812.977 1.00 27.81A C

ATOM 1454CD1LEUA 26017.873 15.69513.983 1.00 23.72A C

ATOM 1455CD2LEUA 26015.651 16.53613.218 1.00 26.71A C

ATOM 1456C LEUA 26017.686 13.22911.112 1.00 28.84A C

ATOM 1457O LEUA 26018.151 12,4D011,893 1.00 29.71A O

ATOM 1458N ARGA 26116.671 12.97210.296 1.00 28.87A N

ATOM 1459CA ARGA 26115.982 11.68710.279 1.00 28.79A C

ATOM 1460CB ARGA 26114.830 11,7519,274 1.00 28.10A C

ATOM 1461CG ARGA 26114.034 10.4759.182 1.00 27.04A C

ATOM 1462CD ARGA 26112.768 10.6648.376 1.00 26.43A C

ATOM 1463NE ARGA 26112.232 9.357 8.015 1.00 25.81A N

ATOM 1464CZ ARGA 26111.504 8.594 8,820 1.00 24.67A C

ATOM 1465NH1ARGA 26111.200 9.009 10.043 1.00 26.17A N

ATOM 1466NH2ARGA 26111.119 7.399 8.413 1.00 25.59A N

ATOM 1467C ARGA 26116.855 10.4639.984 1.00 29.57A C

ATOM t468O ARGA 26116.677 9.398 10.585 1.00 28.88A O

ATOM 1469N LYSA 26217.785 10.5959.047 1.00 30.02A N

ATOM 1470CA LYSA 26218.634 9.468 8.731 1.00 87 A C

ATOM 1471CB LYSA 26219.439 9.734 7.453 1.00 . A C
ATOM 1472CG LYSA 26220.228 8.510 6.961 1.00 31.17A C
35.37 ATOM 1473CD LYSA 26221.124 8.847 5.763 1.00 36 A C

ATOM 1474CE LYSA 26221.940 7.651 5,322 1.00 . A C
36.15 ATOM 1475NZ LYSA 26221.097 6.478 4.972 1.00 35.94A N
ATOM 1476C LYSA 26219.559 9,178 9.918 1.00 29 A C

ATOM 1477O LYSA 26219.729 8.026 10.287 1.00 , A O

ATOM 1478N META 26320.131 10.21910.521 1.00 . A N
29.00 ATOM 1479CA META 26321.021 10.04811.672 1.00 29.24A C
ATOM 1480CB META 26321.654 11.38712.090 1.00 29 A C

ATOM 1481CG META 26322.610 12,00611.066 1.00 . A C
ATOM 1482SD META 26323.567 13.42711,706 1.00 29.31A S
ATOM 1483CE META 26322.406 14.81511.499 1.00 32.86A C

ATOM 1484C META 26320.272 9.443 12,865 1.00 . A C
29.82 ATOM 1485O META 26320.765 8.510 13.517 1.00 29.66A O
ATOM 1486N VALA 26419.079 9.958 13.147 1.00 28.15A N
ATOM 1487CA VALA 26418.299 9.436 14.265 1.00 27.49A C
ATOM 1488CB VALA 26416.976 10.24214.462 1.00 27.30A C

ATOM 1489CG1VALA 26416.056 9.507 15.424 1.00 25.85A C
ATOM 1490CG2VALA 26417.287 11.63714.989 1.00 23 A C

ATOM 1491C VALA 26417.989 7,945 14.049 1.00 . A C
ATOM 1492O VALA 26418.046 7.154 14.988 1.00 26.63A O
ATOM 1493N ILEA 26517.675 7.565 12.816 1.00 26.74A N
ATOM 1494CA ILEA 26517.382 6.166 12.503 1 25.59A C

ATOM 1495CB ILEA 26516.842 5.998 11.046 . . A C
ATOM 1496CG2ILEA 26516.783 4.522 10.663 1.00 24.55A C
1.00 24.31 ATOM1497CG1ILEA 26515.463 6.655 10.910 1.00 23.90 A C

ATOM1498CD1ILEA 26514.844 6.547 9.499 1.00 23.93 A C

ATOM1499C ILEA 26518.646 5.322 12.655 1.00 27.80 A C

ATOM1500O ILEA 26518.609 4.218 13.205 1.00 29.88 A O

ATOM1501N ASPA 26619.768 5.838 12.167 1.00 28.71 A N

ATOM1502CA ASPA 26621.030 5.115 12.261 1.00 30.15 A C

ATOM1503CB ASPA 26622.142 5.874 11.528 1.00 30.66 A C

ATOM1504CG ASPA 26622.040 5.746 10.019 1.00 32.85 A C

ATOM1505ODtASPA 26622.655 6.576 9.311 1.00 34.49 A O

ATOM1506OD2ASPA 26621.356 4.810 9.542 1.00 32.28 A O

ATOM1507C ASPA 26621.448 4.892 13.708 1.00 29.98 A C

ATOM1508O ASPA 26622.018 3.852 14.041 1.00 30.01 A O

ATOM1509N ILEA 26721.157 5.869 14.556 1.00 29.02 A N
' ATOM1510CA fLEA 26721.526 5.791 15.954 1.00 29.50 A C

ATOM1511CB ILEA 26721.454 7.192 16.632 1.00 28.39 A C

ATOM1512CG2ILEA 26721.718 7.082 18.141 1.00 27.00 A C

ATOM1513CGtILEA 26722 8.121 15.995 1.00 26.25 A C

ATOM1514CD1ILEA 267_ 9.512 16.583 1.00 24.39 A C
22.496 ATOM1515C ILEA 26720.673 4.808 16.738 1.00 31.72 A C

ATOM1516O ILEA 26721.198 3.948 17.444 1.00 31.97 A O

ATOM1517N VALA 26819.358 4.921 16.620 1.00 31.99 A N

ATOM1518CA VALA 26818.497 4.019 17.361 1.00 31.45 A C

ATOM1519CB VALA 26817.014 4.476 17.274 1.00 31.37 A C

ATOM1520CG1VALA 26816.126 3.558 18.089 1.00 29.93 A C

ATOM1521CG2VALA 26816.879 5.896 17.786 1.00 30.48 A C

ATOM1522C VALA 26818.632 2.553 16.912 1.00 31.97 A C
i ATOM15230 VALA 26818.537 1.643 17.736 1.00 31.75 A O

ATOM1524N LEUA 26918.849 2.304 15.620 1.00 32.32 A N

ATOM1525CA LEUA 26918.977 0.916 15.187 1.00 32.00 A C

ATOM1526CB LEUA 26918.998 0.802 13.668 1.00 29.91 A C

ATOM1527CG LEUA 26917.715 1.120 12.886 1.00 30.24 A C

ATOM1528CD1LEUA 26917.988 0.896 11.399 1.00 26.00 A C

ATOM1529CD2LEUA 26916.546 0.243 13.356 1.00 27.10 A C

ATOM1530C LEUA 26920.261 0.343 15.787 1.00 34.15 A C

ATOM1531O LEUA 26920.352 -0.84716.077 1.00 34.31 A O

ATOM1532N ALAA 27021.244 1.205 16.001 1.00 35.23 A N

ATOM1533CA ALAA 27022.493 0.769 16.591 1.00 37.06 A C

ATOM1534CB ALAA 27023.574 1.818 16.354 1.00 36.80 A C

ATOM1535C ALAA 27022.384 0.447 18.094 1.00 37.91 A C

ATOM1536O ALAA 27023.375 0.053 18.699 1.00 38.21 A O

ATOM1537N THRA 27121.206 0.616 18.704 1.00 38.60 A N

ATOM1538CA THRA 27121.062 0.290 20.133 1.00 38.59 A C

ATOM1539CB THRA 27119.936 1.075 20.858 1.00 37.35 A C

ATOM1540OG1THRA 27118.669 0.756 20.271 1.00 36.93 A O

ATOM1541CG2THRA 27120.194 2.561 20.811 1.00 36.42 A C

ATOM1542C THRA 27120.734 -1.18620.290 1.00 39.88 A C

ATOM1543O THRA 27120.781 -1.72921.399 1.00 41.49 A O

ATOM1544N ASPA 27220.371 -1.81919.180 1.00 39.61 A N

ATOM1545CA ASPA 27220.075 -3.24119.177 1.00 41.87 A C

ATOM1546CB ASPA 27219.658 x.695 17.774 1.00 41.58 A C

ATOM1547CG ASPA 27219.199 -5.13817.745 1.00 43.32 A C

ATOM1548OD1ASPA 27219.802 -5.95918.476 1.00 42.16 A O

ATOM1549OD2ASPA 27218.245 -5.45316.993 1.00 42.44 A O

ATOM1550C ASPA 27221.393 -3.91919.568 1.00 43.16 A C

ATOM1551O ASPA 27222.439 -3.62618.992 1.00 42.82 A.O

ATOM1552N META 27321.346 -4.81420.548 1.00 45.0_6A N

ATOM1553CA META 27322.551 -5.49921.012 1.00 45.78 A C

ATOM1554CB META 27322.242 -6.34022.256 1.00 47.29 A C

ATOM1555CG META 27322.103 -5.52623.522 1.00 49.01 A C

ATOM1556SD META 27323.607 -4.58923.852 1.00 53.74 A S

ATOM1557CE META 27324.708 -5.92124.378 1.00 51.87 A C

ATOM1558C META 27323.200 -6.38319.958 1.00 46.17 A C

ATOM1559O META 27324.415 -6.58819.985 1.00 46.80 A O

ATOM1560N SERA 27422.398 -6.90119.031 1.00 45.73 A N

ATOM1561CA SERA 27422.921 -7.76317.989 1.00 45.21 A C

ATOM1562CB SERA 27421.779 -8.37517.165 1.00 45.95 A C

ATOM1563OG SERA 27421.097 -7.40516.395 1.00 47.16 A O

ATOM1564C SERA 27423.902 -7.02117.087 1.00 44.69 A C

ATOM1565O SERA 27424.662 -7.64816.357 1.00 45.85 A O

ATOM1566N LYSA 27523.897 -5.69217.145 1.00 44.06 A N

ATOM1567CA LYSA 27524.818 -4.88616.343 1.00 43.84 A C

ATOM1568CB LYSA 27524.159 -3.58215.871 1.00 43.87 A C

ATOM1569CG LYSA 27522.812 -3.72015.173 1.00 44.10 A C

ATOM1570CD LYSA 27522.923 -4.51813.895 1.00 45.01 A C

ATOM1571CE LYSA 27521.555 -4.70613.262 1.00 45.44 A C

ATOM1572NZ LYSA 27521.612 5.701 12.157 1.00 45.76 A N

ATOM1573C LYSA 27526.016 -4.50617.212 1.00 44.10 A C

ATOM1574O LYSA 27526.961 -3.56816.740 1.00 43.24 A O

ATOM1575N HISA 27625.982 -4.90018.481 1.00 43.99 A N

ATOM1576CA HISA 27627.052 -4.52919.401 1.00 45.36 A C

ATOM1577CB HISA 27626.828 -5.15620.777 1.00 45.35 A C

ATOM1578CG HISA 27627.930.-4.86921.746 1.00 47.12 A C

ATOM1579CD2HISA 27628.801 -5.69422.380 1.00 46.35 A C

ATOM1580ND1HISA 27628.296 -3.58622.101 1.00 46.91 A N

ATOM1581CE1HISA 27629.342 -3.63422.908 1.00 46.71 A C

ATOM1582NE2HISA 27629.668 -4.90023.093 1.00 46.48 A N

ATOM1583C HIS A 27628.477-4.82118.942 1.00 45.97 A C
ATOM1584O HIS A 27629.2893.903 18.835 1.00 45.44 A O

ATOM1585N MET A 27728.784-6.08818.678 1.00 47.63 A N

ATOM1586CA MET A 27730.128-6.48918.250 1.00 49.52 A C

ATOM1587CB MET A 27730.171-7.95317.883 1.00 51.43 A C
ATOM1588CG MET A 27730.001-8.89819.071 1.00 54.47 A C

ATOM1589SD MET A 27731.112-8.54320.468 1.00 57.42 A S

ATOM1590CE MET A 27730.063-9.01721.883 1.00 56.99 A C
ATOM1591C MET A 27730.658-5.64617.083 1.00 50.07 A C
ATOM1592O MET A 27731.725-5.03217.177 1.00 50.57 A O

ATOM1593N ASN A 27829.917-5.62515.982 1.00 50.61 A N

ATOM1594CA ASN A 27830.352-4.86814.817 1.00 50.95 A C

ATOM1595CB ASN A 27829.347-5.03713.675 1.00 52.82 A C

ATOM1596CG ASN A 27829.359-6.44713.100 1.00 55.02 A C

ATOM1597OD1ASN A 27830.406-6.94712.684 1.00 55.87 A O

ATOM1598ND2ASN A 27828.198-7.09613.078 1.00 55.89 A N

ATOM1599C ASN A 27830.5833.390 15.123 1.00 50.54 A C

ATOM1600O ASN A 27831.548-2.80114.631 1.00 51.41 A O

ATOM1601N LEU A 27929.717-2.78815.936 1.00 48.78 A N
ATOM1602CA LEU A 27929.884-1.38116.284 1.00 47.85 A C

ATOM1603CB LEU A 27928.749-0.89517.195 1.00 48.61 A C

ATOM1604CG LEU A 27927.6890.070 16.656 1.00 47.87 A C

ATOM1605CD1LEU A 27926.8320.557 17.824 1.00 47.56 A C

ATOM1606CD2LEU A 27928.3461.248 15.968 1.00 47.56 A C

ATOM1607C LEU A 27931.205-1.18317.012 1.00 47.23 A C

ATOM1608O lEU A 27931.985-0.29316.664 1.00 46.74 A O

ATOM1609N LEU A 28031.440-2.01818.024 1.00 46.74 A N

ATOM1610CA LEU A 28032.658-1.95918.834 1.00 46.77 A C

ATOM1617CB LEU A 28032.604-3.00919.949 1.00 45.81 A C

ATOM1612CG LEU A 28033.812-0.08420.888 1.00 44.80 A C

ATOM1613CD1LEU A 28033.984-1.77421.626 1.00 44.05 A C

ATOM1614CD2LEU A 28033.620-4.21921.869 1.00 44.76 A C

ATOM1615C LEU A 28033.901-2.18717.987 1.00 47.26 A C

ATOM1616O LEU A 28034.918-1.50418.149 1.00 47.04 A O

ATOM1617N ALA A 28133.813-3.15217.081 1.00 47.97 A N

ATOM1618CA ALA A 28134.929-3.45616.201 1.00 49.43 A C

ATOM1619CB ALA A 28134.552-4.58515.244 1.00 48.27 A C

ATOM1620C ALA A 28135,321-2.20615.417 1.00 50.68 A C

ATOM1621O ALA A 28136.490-1.80915.417 1.00 51.41 A O

ATOM1622N ASP A 28234.342-1.57914.765 1.00 51.48 A N

ATOM1623CA ASP A 28234.607-0.37813.974 1.00 52.02 A C

ATOM1624CB ASP A 28233.3530.056 13.209 1.00 53.76 A C

ATOM1625CG ASP A 28232.776-1.06012.355 1.00 55.82 A C

ATOM1626OD1ASP A 28233.570-1.84611.784 1.00 56.43 A O

ATOM1627OD2ASP A 28231.531-1.14712,245 1.00 56.67 A O

ATOM1628C ASP A 28235.1130.773 14.834 1.00 51.41 A C

ATOM1629O ASP A 28235.9081.591 14.377 1.00 50.55 A O

ATOM1630N LEU A 28334.6480.838 16.079 1.00 52.21 A N

ATOM1631CA LEU A 28335.0861.888 16.991 1.00 52.69 A C

ATOM1632CB LEU A 28334.2381.879 18.268 1.00 50.67 A C

ATOM1633CG LEU A 28334.5912.943 19.311 1.00 48.68 A C

ATOM1634CD1LEU A 28334.4694.320 18.687 1.00 49.03 A C

ATOM1635CD2LEU A 28333.6842.816 20.515 1.00 48.17 A C

ATOM1636C LEU A 28336.5651.669 17.336 1.00 54.31 A C

ATOM1637O LEU A 28337.345'2.623 17.378 1.00 54.38 A O

ATOM1638N LYS A 28436.9480.416 17.587 1.00 56.00 A N

ATOM1639CA LYS A 28438.3470.111 17.893 1.00 58.51 A C

ATOM1640CB LYS A 28438.522-1.36418.285 1.00 58.01 A C

ATOM1641CG LYS A 28438.159-1.63919.731 1.00 5_8.55A C

ATOM1642CD LYS A 28438.088-3.11420.057 1,00 5 A C

ATOM1643CE LYS A 28437.662-3.30021.506 1.00 _ A C
_ _ 60.01 ATOM1644NZ LYS A 28437.490-4.72821.875 1.00 61.32 A N

ATOM1645C LYS A 28439.1820.418 16.660 1.00 59.85 A C

ATOM1646O LYS A 28440.2621.011 16.757 1.00 59.14 A O

ATOM1647N THR A 28538.6630.018 15.500 1.00 60.91 A N

ATOM1648CA THR A 28539.3420.258 _ 14.2371.00 62.66 A C

ATOM1649CB THR A 28538.555-0.34 0 ___ 1.00 62.62 _ C
13.052 A

ATOM1650OG1THR A 28538.558-1.769_ 1.00 63.03 A O
13,150 ATOM1651CG2THR A 28539_.1810.062 11.126 1.00 63.22 A C

ATOM1652C THR A 28539.5001.760 14.044 1.00 _ A C
64.20 ATOM16530 THR A 28540.4762.218 13.451 1.00 64.80 A O

I 1654N MET A 28638.5492.537 _ 1.00 65.73 A N
ATOM - 14.550 A 1655CA MET A 28638.6573.981 14.415 1.00 67.67 A C
M

ATOM1656CB MET A _2_8637.3324.686 14.709 1.00 67.73 A C

ATOM1657CG MET A 28637.4536.198 14.580 1.00 67.85 A C

ATOM1658SD MET A 28635.9297.090 14.881 1.00 69.15 A S

ATOM1659CE MET A 28634.9926.671 13.402 1.00 68.20 A C

ATOM1660C MET A 28639.7094.497 15.373 1.00 68.16 A C

ATOM1661O MET A 28640.5545.298 14.998 1.00 68.45 A O

ATOM1662N VAL A 28739.6504.028 16.612 1.00 69.78 A N

ATOM1663CA VAL A 28740.5994.450 17.637 1.00 71.53 A C
I 1664CB VAL A 28740.2793.771 18.986 1.00 71.41 A C
ATOM1665CG1VAL A 28741.3354.124 20.011 1.00 71.49 A C
ATOM

ATOM1666CG2VAL A 28738.9004.219 19.467 1.00 70.95 A C

ATOM1667C VAL A 28742.0384.135 17.229 1.00 72.61 A C

I 1668O VAL A 28742.9754.800 17.675 1 nn 7~ o n ATOMI I / I I I an [

ATOM1669N GLU A 28842.208 3.132 16.372 1.00 74.07 A N

ATOM1670CA GLU A 28843.535 2.749 15.902 1.00 75.79 A C

ATOM1671CB GLU A 28843.497 1.357 15.270 1.00 76.39 A C

ATOM1672CG GLU A 28843.031 0.254 16.210 1.00 77.99 A C

ATOM1673CD GLU A 28842.871 -1.08515.507 1.00 79.05 A C
~

ATOM1674OE1GLU A 28843.890 -1.64415.049 1.00 80.32 A O

ATOM1675OE2GLU A 28841.730 -1.57915.400 1.00 79.26 A O

ATOM1676C GLU A 28844.015 3.774 14.869 1.00 76.49 A C

ATOM1677O GLU A 28845.017 4.458 15.078 1.00 76.25 A O

ATOM1678N THR A 28943.286 3.875 13.762 1.00 77.64 A N

ATOM1679CA THR A 28943.614 4.814 12.693 1.00 78.87 A C

ATOM1680CB THR A 28942.878 4.431 11.384 1.00 79.03 A C

ATOM1681OG1THR A 28941.461 4.571 11.569 1.00 79.05 A O

ATOM1682CG2THR A 28943.188 2.984 10.998 1.00 79.13 A C

ATOM1683C THR A 28943.222 6.251 13.073 1.00 79.59 A C
i ATOM1684O THR A 28943.284 7.165 12.254 1.00 79.73 A O

ATOM1685N LYS A 29042.824 6.42_414.326 1.00 80.87 A N

ATOM1686CA LYS A 29042.396 7.707 14.866 1.00 82.18 A C

ATOM1687CB LYS A 29042.237 7.555 16.383 1.00 81.86 A C

ATOM1688CG LYS A 29042.103 8.835 17.173 1:00 81.45 A C

ATOM1689CD LYS A 29042.091 5.508 18.658 1.00 81.60 A C

ATOM1690CE LYS A 29042.260 9.739 19.524 1.00 81.45 A C

ATOM1691NZ LYS A 29042.329 9.389 20.971 1.00 80.91 A N

ATOM1692C LYS A 29043.321 8.887 14.553 1.00 83.45 A C

ATOM1693O LYS A 29044.490 8.891 14.921 1.00 83.74 A O

ATOM1694N LYS A 29142.785 9.888 13.862 1.00 84.88 A N

ATOM1695CA LYS A 29143.543 11.08813.528 1.00 86.40 A C

ATOM1696CB LYS A 29143.337 11.47012.057 1.00 86.58 A C

ATOM1697CG LYS A 29144.478 12.29811.470 1.00 87.47 A C

ATOM1698CD LYS A 29144.425 12.3679.946 1.00 88.10 A C

ATOM1699CE LYS A 29145.720 12.9669.391 1.00 88.76 A C

ATOM1700NZ LYS A 29145.731 13.0627.901 1.00 88.77 A N

ATOM1701C LYS A 29143.013 12.18214.457 1.00 87.17 A C

ATOM1702O LYS A 29141.831 12.18014.791 1.00 86.94 A O

ATOM1703N VAL A 29243.863 13.11314.881 1.00 88.37 A N

ATOM1704CA VAL A 29243.396 14.14215.813 1.00 89.34 A C

ATOM1705CB VAL A 29243.718 13.71417.281 1.00 59.07 A C

ATOM1706CG1VAL A 29242.836 94.45718.272 1.00 88.88 A C

ATOM1707CG2VAL A 29243.529 12.21017.434 1.00 88.94 A C

ATOM1708C VAL A 29243.951 15.55115.590 1.00 90.23 A C

ATOM1709O VAL A 29244.349 15.93214.478 1.00 90.08 A O

ATOM1710N THR A 29343.941 16.30516.696 1.00 91.60 A N

ATOM1711CA THR A 29344.409 17.68516.842 1.00 93.29 A C

ATOM1712CB THR A 29345.937 17.77616.632 1.00 93.64 A C

ATOM1713OGtTHR A 29346.287 17.23015.356 1.00 94.06 A O

ATOM1714CG2THR A 29346.657 17.02017.753 1.00 93.66 A C

ATOM1715C THR A 29343.753 18.84416.096 1.00 94.07 A C

ATOM1716O THR A 29342.677 18.71315.502 1.00 94.13 A 0 ATOM1717N SER A 29444.449 19.98116.165 1.00 94.96 A N

ATOM1718CA SER A 29444.073 21.28415.601 1.00 95.53 A C

ATOM1719CB SER A 29442.906 21.20414.612 1.00 95.82 A C

ATOM1720OG SER A 29442.612 22.49614.103 1.00 96.35 A O

ATOM1721C SER A 29443.636 22.05716.832 1.00 95.88 A C

ATOM1722O SER A 29443.564 23.29616.844 1.00 96.25 A O

ATOM1723N SER A 29543.358 21.27117.868 1.00 __95_.4_6A N

ATOM1724CA SER A 29542.920 21.74719.175 1.00 94.51 A C

ATOM1725CB SER A 29541.424 22.09919.136 1.00 94.63 A C

ATOM1726OG SER A 29540.935 22.17417.801 1.00 93.96 A O

ATOM1727C SER A 29543.147 20.58720.158 1.00 93.70 A C

ATOM1728O SER A 29542.953 20.73321.367 1.00 93.65 A O

ATOM1729N GLY A 29643.559 19.43919.613 1.00 92.57 A N

ATOM1730CA GLY A 29643.779 18.23620.403 1.00 90.71 A C

ATOM1731C GLY A 29642.484 17.43420.358 1.00 89.46 A C

ATOM1732O GLY A 29642 16.36120.962 1.00 89.30 A O

ATOM1733N VAL A 297_ 17.98519.619 __1._0087.87 A N
41.521 ATOM1734CA VAL A 29740.201 17.39519.459 1.00 86_.0_2A C

ATOM1735CB VAL A 29739.132 18.50319.303 1.00 86.00 A C

ATOM1736CG1VAL A 29737.779 17.88019.064 1.00 85.80 A C

ATOM1737CG2VAL A 29739.091 19.38420.556 1.00 85.51 A C

ATOM1738C VAL A 29740.107 16.45218.259 1.00 84.77 A C

ATOM1739O VAL A 29740.760 16.65317.235 1.00 84.97 A O

ATOM1740N LEU A 29839.276 15.42618.398 1.00 82.88 A N

ATOM1741CA LEU A 29839.069 14.42817.356 1.00 81.04 A C

ATOM1742CB LEU A 29837.918 13.50817.764 1.00 81.36 A C

ATOM1743CG LEU A 29837.755 12.19816.993 1.00 81.97 A C

ATOM1744CD1LEU A 29838.956 11.28817.243 1.00 82.03 A C

ATOM1745CD2LEU A 29836.475 11.52117.448 1.00 82.34 A C

ATOM1746C LEU A 29838.780 15.040__15.9801.00 79.62 A C

ATOM1747O LEU A 298_38_.19616.11915.870 1.00 79.29 A O

ATOM1748N LEU A 29939.190 14.33814.929 1.00 77.90 A N

ATOM1749CA LEU A 29938.979 14.80813.569 1.00 76.31 A C

ATOM1750CB LEU A 29940.333 15.01612.877 1.00 76.82 A C

ATOM1751CG LEU A 29940.404 15.77111.542 1.00 77.19 A C

ATOM1752CD1LEU A 29941.846 16.21011.305 1.00 77.22 A C

ATOM1753CD2LEU A 29939.902 14.90210.389 1.00 76.92 A C

ATOM1754C LEU A 29938.147 13.78912.804 1.00 75.01 A C

ATOM1755O LEU A 29938.62812.70012.491 1.00 74.67 A O

ATOM1756N LEU A 30036.90014.14512.504 1.00 73.43 A N
ATOM1757CA LEU A 30036.00513.24711.779 1.00 72.31 A C

ATOM1758CB LEU A 30034.68713.09412.536 1.00 71.77 A C

ATOM1759CG LEU A 30034.83212.49413.937 1.00 71.21 A C

ATOM1760CD1LEU A 30033.46312.36614.589 1.00 70.37 A C
ATOM1761CD2LEU A 30035.50811.13313.841 1.00 70.67 A C

ATOM1762C LEU A 30035.74013.72810.360 1.00 71.95 A C

ATOM1763O LEU A 3D035.14214.78210.145 1.00 71.52 A O

ATOM1764N ASP A 30136.18712.9299.397 1.00 71.63 A N

ATOM1765CA ASP A 30136.04613.2447.952 1.00 71.03 A C

ATOM1766CB ASP A 30137.00712.3687.170 1.00 72.93 A C
ATOM1767CG ASP A 30136.92812.6405.679 1.00 74.77 A C

ATOM1768OD1ASP A 30137.19611.7084.887 1.00 74.66 A O

ATOM1769OD2ASP A 30136.60413.7885.300 1.00 76.66 A O

ATOM1770C ASP A 30134.62313.0727.449 1.00 69.31 A C

ATOM1771O ASP A 30133.77313.9467.615 1.00 69.67 A O

ATOM1772N ASN A 30234:38011.9316.813 1.00 66.94 A N
ATOM1773CA ASN A 30233.08711.6156.224 1.00 64.87 A C

ATOM1774CB ASN A 30233.24910.4415.254 1.00 65.84 A C

ATOM1775CG ASN A 30233.9899.266 5.876 1.00 66.89 A C

ATOM1776OD1ASN A 30233.6548.808 6.972 1.00 67.22 A O

ATOM1777ND2ASN A 30234.9968.767 5.169 1.00 68.12 A N

ATOM1778C ASN A 30231.96111.2977.213 1.00 62.89 A C
ATOM1779O ASN A 30232.13211.3718.433 1.00 62.06 A O

ATOM1750N TYR A 30330.80910.9326.656 1.00 59.78 A N

ATOM1781CA TYR A 30329.63210.5927.442 1.00 57.72 A C

ATOM1782CB TYR A 30328.39910.4796.526 1.00 56.40 A C
-ATOM7783CG TYR A 30327.10810.1577.258 1.00 54.89 A C

ATOM1784CD1TYR A 30326.52611.0758.132 1.00 54.24 A C

ATOM1785CEiTYR A 30325.35610.7638.833 1.00 54.32 A C

ATOM1786CD2TYR A 30326.4888.917 7.098 1.00 54.61 A C

ATOM1787CE2TYR A 30325.3248.592 7.794 1.00 54.11 A C

ATOM1788CZ TYR A 30324.7659.519 8.660 1.00 54.21 A C

ATOM1789OH TYR A 30323.6289.187 9.360 1.00 53.84 A O

ATOM1790C TYR A 30329.8229.282 8.208 1.00 56.44 A C

ATOM17910 TYR A 30329.5309.212 9.404 1.00 55.92 A O

ATOM1792N SER A 30430.3038.249 7.517 1.00 54.66 A N

ATOM1793CA SER A 30430.5156.948 8,142 1.00 53,32 A C

ATOM1794CB SER A 30431.3566.034 7.248 1.00 53.48 A C

ATOM1795OG SER A 30430.5945.514 6.177 1.00 54.68 A O

ATOM1796C SER A 30431.2137.085 9.479 1.00 51.77 A C

ATOM1797O SER A 30430.9406.326 10.411 1.00 51.09 A O

ATOM1798N ASP A 30532.1138.056 9.571 1.00 49.68 A N

ATOM1799CA ASP A 30532.8618.266 10.798 1.00 48,71 A C

ATOM1800CB ASP A 30534.1559.017 10.493 1.00 48.22 A C

ATOM1801CG ASP A 30535.2558.095 10.003 1.00 49.03 A C

ATOM1802OD1ASP A 30534.9406.991 9.496 1:00 47.28 A O

ATOM1803OD2ASP A 30536.4358.483 10.118 1.00 49.68 A O

ATOM1804C ASP A 30532.0838.999 11.872 1.00 48.37 A C

ATOM1805O ASP A 30532.0328.556 13.023 1.00 48.82 A 0 ATOM1806N ARG A 30631.47410.11711.495 1:0D 46.68 A N

ATOM1807CA ARG A 30630.71510.92012.443 1.00 45.21 A C

ATOM1808CB ARG A 30630.26212.21711.769 1.00 44.83 A C

ATOM1809CG ARG A 30631.36412.86510.945 1.00 45.11 A C

ATOM1810CD ARG A 30630.94814.20810.378 1.0D 43.33 A C

ATOM1811NE ARG A 30630.82415.19411.437 1.00 44.20 A N

ATOM1812CZ ARG A 30630.92816.50411.255 1.00 45.67 A C

ATOM1813NHtARG A 30631.16416.99610.036 1.00 48.08 A N

ATOM1814NH2ARG A 30630.79417.32412.290 1.00 42.49 A N

ATOM1815C ARG A 30629,51410.17713.023 1.00 43.34 A C

ATOM1816O ARG A 30629.30410.18514.230 1.00 43.05 A O

ATOM1517N ILE A 30728.7359.526 12.166 1.00 42.39 A N

ATOM1818CA ILE A 30727.5628.809 12.636 1.00 41.50 A C

ATOM1819CB ILE A 30726.6688.356 11.450 1.00 38.81 A C

ATOM1820CG2ILE A 30727.3837.313 10.615 1.00 39.17 A C

ATOM1821CG1ILE A 30725.3447.800 11.978 1.00 35.80 A C

ATOM1822CD1ILE A 30724.4658.845 12.645 1.00 31.79 A C

ATOM1823C ILE A 30727.9827.600 13.474 1.00 43.12 A C

ATOM1524O ILE A 30727.2887.206 14.413 1.00 42.89 A O

ATOM1825N GLN A 30829.1307.024 13.132 1.00 42.85 A N

ATOM1826CA GLN A 30829.6565.868 13.847 1.00 43.10 A C

ATOM1827CB GLN A 30830.9235.390 13.148 1.00 46.69 A C

ATOM1828CG GLN A 30831.4884.077 13.613 1.00 50.45 A C

ATOM1829CD GLN A 30832.6153.618 12.696 1.00 54.67 A C

ATOM1830OE1GLN A 308' 32.3913.303 11.515 1.00 54.64 A O

ATOM1831NE2GLN A 30833.8383.599 13.227 1.00 54.71 A N

ATOM1832C GLN A 30829.9536.257 15.292 1.00 41.10 A C

ATOM1833O GLN A 30829.5945.535 16.219 1.00 39.42 A O

ATOM1834N VAL A 30930.6077.404 15.471 1.00 39.52 A N

ATOM1835CA VAL A 30930.9337.912 16.798 1.00 38.55 A C

ATOM1836CB VAL A 30931.7809.198 16.707 1.00 38.46 A C

ATOM1837CG1VAL A 30931.8269.910 18.054 1.00 36.76 A C

ATOM1838CG2VAL A 30933.1988.842 16.264 1.00 39.99 A C

ATOM1839C VAL A 30929.6538.201 17.575 1.00 39.03 A C

ATOM1840O VAL A 30929.5157.790 18.719 1.00 39.10 A O

ATOM1841N LEU 31028.716 8.909 16.949 1.00 39.17 A N
.
A

ATOM1842CA LEU A 31027.447 9.227 17.595 1.00 38.18 A C
, ATOM1843CB LEU A 31026.591 10.09616.678 1.00 39.22 A C

ATOM1844CG LEU A 31027.134 11.48216.353 1.00 38.91 A C

ATOM1845CD1LEU A 31026.277 12.08015.237 1.00 40.41 A C

ATOM1846CD2LEU A 31027.116 12.37317.597 1.00 37.70 A C

ATOM1847C LEU A 31026.681 7.957 17.956 1.00 36.88 A C

ATOM1848O LEU A 31026.086 7.882 19.023 1.00 36.61 A 0 ATOM1849N GLN A 31126.691 6.967 17.064 1.00 36.58 A N

ATOM1850CA GLN A 31126.007 5.692 17.314 1.00 36.23 A C

ATOM1851CB GLN A 31126.176 4.728 16.133 1.00 36.76 A C

ATOM1852CG GLN A 31125.457 5.074 14.828 1.00 36.29 A C

ATOM1853CD GLN A 31125.823 4.081 13.724 1.00 35.25 A C

ATOM1854OE1GLN A 31127.003 3.773 13.530 1.00 33.90 A O

ATOM1855NE2GLN A 31124.822 3.579 13.005 1.00 31.71 A N

ATOM1856C GLN A 31126.591 5.014 18.561 1.00 35.83 A C

ATOM1857O GLN A 31125.864 4.468 19.393 1.00 34.41 A O

ATOM1858N ASN A 31227.914 5.023 18.670 1.00 36.34 A N

ATOM1859CA ASN A 31228.562 4.416 19.825 1.00 36.91 A C

ATOM1860CB ASN A 31230.065 4.221 19.564 1.00 39.17 A C

ATOM1861CG ASN A 31230.371 2.875 18.923 1.00 41.01 A C

ATOM1862OD1ASN A 31230.099 1.833 19.508 1.00 43.85 A O

ATOM1863ND2ASN A 31230.929 2.894 17.714 1.00 42.92 A N

ATOM1864C ASN A 31228.336 5.278 21.061 1.00 35.31 A C

ATOM1865O ASN A 31228.198 4.760 22.170 1.00 35.09 A O

ATOM1866N MET A 31328.256 6.589 20.863 1.00 33.77 A N

ATOM1867CA MET A 31328.043 7.506 21.978 1.00 33.99 A C

ATOM1868CB MET A 31328.039 8.945 21.484 1.00 33.69 A C

ATOM1869CG MET A 31328.031 9.951 22.603 1.00 35.94 A C

ATOM1870SD MET A 31327.886 11.65322.031 1.00 39.46 A S

ATOM1871CE MET A 31329.102 11.70220.680 1.00 38.19 A C

ATOM1872C MET A 31326.726 7.197 22.699 1.00 33.28 A C

ATOM1873O MET A 31326.696 7.029 23.917 1.00 __32.95A O

ATOM1874N VAL A 31425.644 7.117 21.937 1.00 32.39 A N

ATOM1875CA VAL A 31424.325 6.811 22.487 1.00 32.40 A C

ATOM1876CB VAL A 31423.231 7.008 21.405 1.00 31.89 A C

ATOM1877CG1VAL A 31421.876 6.549 21.926 1.00 29.38 A C

ATOM1878CG2VAL A 31423.195 8.473 20.993 1.00 29.23 A C

ATOM1879C VAL A 31424.303 5.364 22,989 1.00 32.09 A C

ATOM1880O VAL A 31423.608 5.034 23.944 1.00 32.01 A O

ATOM1881N H1S A 31525.062 4.504 22.323 1.00 32.30 A N

ATOM1882CA HIS A 31525.164 __3._10_722.721 1.00 32.74 A C

ATOM1883CB HIS A 31525.987 2.327 21.691 1.00 32.98 A C

ATOM1884CG HIS A _ __ 0.874 22.015 1.00 32.29 A C
31526.140 ATOM1885CD2HIS A 31527.213 0.054 21.946 1.00 30.39 A C

ATOM1886ND1HIS A 31525.078 0.082 22.396 1.00 32.46 A N

ATOM1887CE1HIS A 31525.488 -1.16422.542 1.00 29.74 A C

ATOM1888NE2HIS A 31526.779 -1.20722.272 1.00 31.47 A N

ATOM1889C HIS A 31525.844 3.049 24.098 1.00 32.55 A C

ATOM1890O HIS A 31525.498 2.212 24.934 1.00 31.29 A O

ATOM1891N CYS A 31626.801 3.949 24.325 1.00 32.59 A N

ATOM1892CA CYS A 31627.490 4.011 25.610 1.00 33.13 A C

ATOM1893CB CYS A 31628.752 4.880 25.522 1.00 32.21 A C

ATOM1894SG CYS A 31630.173 4,091 24.689 1.00 34.93 A S

ATOM1895C CYS A 31626.563 4.575 26.691 1.00 33.44 A C

ATOM1896O CYS A 31626.623 4.154 27.848 1.00 33.51 A O

ATOM1897N ALA A 3172 5.522 26.315 1.00 32.63 A N
5.706 ATOM1898CA ALA A 317_ __ _ 1.00 _ A C
24.795 6.132 27.277 3 1.81 ATOM1899CB ALA A 31724.129 7.381 26.670 1.00 ____ A C
_ 30.74 ATOM1900C ALA A 31723.742 5.108 _ 1.00 32.28 A C
27.664 ATOM1901O ALA A _ 23.277 5.077 28.792 1.00 33.58 A O

ATOM1902N ASP A 31823.372 4.263 26.717 1.00 33.21 A N

ATOM1903CA ASP A 31822.367 3.241 26.963 1.00 35.23 A C

ATOM1904CB ASP A 31821.910 2.664 25.616 1.00 34.16 A C

ATOM1905CG ASP A 31820.647 1.834 25.720 1.00 34.59 A C
ATOM1906OD2ASP A 31820.596 0.800 25.027 1.00 34.34 A O

ATOM1907C ASP A 31822.949 2.146 27.877 1.00 35.93 A C

ATOM1908O ASP A 31822.223 1.517 28.641 1.00 36.40 A O

ATOM1909OD1ASP A 31819.693 2.212 26.450 1.00 36.16 A O

ATOM1910N LEU A 31924.259 1.926 27.802 1.00 36.23 A N

ATOM1911CA LEU A 31924.900 0.921 28.645 1.00 36.47 A C

ATOM1912CB LEU A 31925.717 -0.04827.795 1.00 37.19 A C

ATOM1913CG LEU A 31925.022 -0.73026.618 1.00 38.46 A C

ATOM1914CDtLEU A 31925.880 -1.87026.143 1.00 38.14 A C

ATOM1915CD2LEU A 31923.658 -1.24727.029 1.00 39.10 A C

ATOM1916C LEU A 31925.812 1.613 29.656 1.00. 36.60 A C

ATOM1917O LEU A 31926.894 1.117 29.983 1.00 36.20 A O

ATOM1918N SER A 32025.357 2.757 30.159 1.00 36.21 A N

ATOM1919CA SER A 32026.133 3.549 31.105 1.00 35.11 A C

ATOM1920CB SER A 32025.934 5.029 30.819 1.00 34.59 A C

ATOM1921OG SER A 32024.649 5.429 31.257 1.00 31.05 A O

ATOM1922C SER A 32025.794 3.325 32.568 1.00 36.04 A C

ATOM1923O SER A 32026.537 3.772 33.442 1.00 35.11 A O

ATOM1924N ASN A 32124.671 2,668 32.849 1.00 37.38 A N

ATOM1925CA ASN A 32124.289 2.455 34.236 1.00 38.46 A C

ATOM1926CB ASN A 32122.931 1.732 34,330 1.00. 40.00 A C

ATOM 927 G SN 3 2122,931 0.377 33.667 1.00 42.79 C

I A 2123.227 -0.63934.304 1.00 O
ATOM 928 OD1SN 3 2122.605 0.346 32.375 1.00 44.09 A N
1 929 A ASNA 32125.372 1.762 35.066 1.00 44.32 A C
ATOM 1930ND2ASN3 32125.556 2.099 36.232 1.00 38.72 A O
1 1931C ASNA 32226.137 0.825 34,471 1.00 38.59 A N
ATOM 1932O PROA 32225.999 0.144 33.171 1.00 39.36 A C
ATOM 1933N PROA 32227.174 0.172 35.274 1.00 39.60 A C
ATOM 1934CD PROA 34 1 40.26 A C
ATOM CA A 383 D0 39.60 ATOM

ATOM 1935CB PROA 32227.632 -0.985. . 40.48 A C
ATOM 1936CG PROA 32226.448 -1.24733.507 1.00 40.42 A C
ATOM 1937C PROA 32228,329 1.111 35.607 1.00 41.68 A O
ATOM 1938O PROA 32229.169 0.787 36.451 1.00 39.80 A N
ATOM 1939N THRA 32328.363 2.269 34.950 1.00 39.92 A C
ATOM 1940CA THRA 32329.433 3.247 35.160 1.00 40.47 A C
ATOM 1941CB THRA 32329.900 3.884 33.818 1.00 40.99 A O
ATOM 1942OG1THRA 32328.957 4.882 33.394 1.00 40.13 A C
14 733 1.00 ATOM 1943CG2THRA 32330.011 2.5 . 1.00 40.46 A C
ATOM 1944C THRA 32329:034 4.381 36.088 1.00 40.30 A O
ATOM 1945O THRA 32329.839 5.275 36.374 1.00 40.56 A N
ATOM 1946N LYSA 32427.795 4.361 36.560 1.00 42.29 A C
ATOM 1947CA LYSA 32427.341 5.424 37.442 1.00 41.85 A C

ATOM 1948CB LYSA 32425.842 . . 1.00 41.55 A C
ATOM 1949CG LYSA 32425.453 6.043 36.813 1.00 40.02 A C
ATOM 1950CD LYSA 32425.906 7.443 35.420 1,00 39.01 A C
ATOM 1951CE LYSA 32425,565 7.726 33.962 1.00 39.15 A N
ATOM 1952NZ LYSA 32424.107 7.523 33.690 1.00 43.81 A C
ATOM 1953C LYSA 32427.608 5.074 38.905 1.00 43.52 A O
ATOM 1954O LYSA 32427.855 3.906 39.243 1.00 44.46 A N
ATOM 1955N PROA 32527.585 6.087 39.791 1.00 44.50 A C

ATOM 1956CD PROA 32527.474 . . 1.00 44.72 A C
ATOM 1957CA PROA 32527.819 5.819 41.206 1.00 44.95 A C
ATOM 1958CB PROA 32527.384 7.117 41.865 1.0D 44.28 A C
ATOM 1959CG PROA 32527.919 8.128 40.893 1.00 45.11 A C
ATOM 1960C PROA 32526.978 4.624 41.614 1.00 45.62 A O
ATOM 1961O PROA 32525.834 4.472 41.178 1.00 45.02 A N
ATOM 1962N LEUA 32627.563 3.772 42.442 1.00 44.46 A C
ATOM 1963CA , A 32626.917 2.553 42.894 1.00 44.30 A C

ATOM 1964CB LEUA 32627.749 . . 1.00 45.25 A C
ATOM 1965CG LEUA 32627.381 . 0.50144.360 1.00 44.54 A C
ATOM 1966CD1LEUA 32627.584 -0.38043.134 1.00 45.19 A C
ATOM 1967CD2LEUA 32628.235 0.031 45.535 1.00 44.30 A C
ATOM 1968C LEUA 32625.454 2.675 43.323 1.00 44.52 A O
ATOM 1969O LEUA 32624.639 1.812 42.984 1.00 44.61 A N
ATOM 1970N GLNA 32725.110 3.724 44.066 1.0O 45.38 A C
ATOM 1971CA GLNA 32723.723 3.885 44.499 1.00 47.58 A C
ATOM 1972CB GLNA 32723.548 5.132 45.370 1.00 51.08 A C
ATOM 1973CG GLNA 32722.092 5:371 45.765 1.00 54.22 A C

ATOM 1974CD GLNA 32721.936 . . 1.00 57.69 A O
ATOM 1975OE1GLNA 32722.421 7.518 46.786 1.00 55.79 A N
ATOM 1976NE2GLNA 32721.251 5.994 47.948 1.00 44.06 A C
ATOM 1977C GLNA 32722.778 3.968 43.306 1.00 44.03 A O
ATOM 1978O GLNA 32721.636 3.512 43.382 1.00 42.12 A N
ATOM 1979N LEUA 32823.250 4.559 42.212 1.00 41.47 A C
ATOM 1980CA LEUA 32822.435 4.664 41.006 1.00 39.50 A C
ATOM 1981CB LEUA 32823.002 5.724 40.060 1.00 36.83 A C
ATOM 1982CG LEUA 32822.626 7.170 40.362 1.00 37.00 A C
ATOM 1983CD1LEUA 32823.309 8.089 39.369 1.00 36.38 A C
ATOM 1984CD2LEUA 32821.119 7.324 40.290 00 41.10 A C

ATOM 1985C LEUA 32822.414 .3 . . 42.09 A O
ATOM 1986O LEUA 32821.350 2.751 40.035 1.00 41.02 A N
ATOM 1987N TYRA 32923.603 2.812 40.013 1,0D 40.75 A C
ATOM 1988CA TYRA 32923.758 1.532 39.336 1.00 41.01 A C
ATOM 1989CB TYRA 32925.232 1.130 39.386 1.00 42.15 A C
ATOM 1990CG TYRA 32925.589 -0.18138.716 1.00 41.75 A C
ATOM 1991CD1TYRA 32924.764 -0.75937.750 1.00 42.44 A C
ATOM 1992CE1TYRA 32925.119 -1.95937.124 1.00 42.13 A C
ATOM 1993CD2TYRA 32926.779 -0.83339.039 1.00 42.27 A C
ATOM 1994CE2TYRA 32927.140 -2.02138.421 1,00 42.62 A C
ATOM 1995CZ TYRA 32926.314 -2.58037.472 1.00 43.27 A O
ATOM 1996OH TYRA 32926.695 -3,76336.879 1.00 41.21 A C
ATOM 1997C TYRA 32922.859 0.434 39.921 1.00 40.85 A O
ATOM 1998O TYRA 32922.114 -0.22639.182 1.00 40.59 A N
ATOM 1999N ARGA 33022.898 0.243 41.239 1.00 40.63 A C
ATOM 2000CA ARGA 33022.066 -0.79941.840 1.00 42.34 A C
ATOM 2001CB ARGA 33022.368 -0.93143.335 1.00 44.73 A C
ATOM 2002CG ARGA 33023.730 -1.58943.619 1.00 45.80 A C
ATOM 2003CD ARGA 33023.608 -2.70044.659 1.00 47.52 A N
ATOM 2004NE ARGA 33023.387 -2.95145.992 1.00 46.66 A C
ATOM 2005CZ ARGA 33022.932 -2.83747.035 1.00 44.93 A N
ATOM 2006NH1ARGA 33022.634 x.126 46.923 1.00 47.32 A N
ATOM 2007NH2ARGA 33022.782 -2.22248.199 1.00 39.77 A C
ATOM 2008C ARGA 33020.566 -0.59641.598 1.00 39.30 A O
ATOM 2009O ARC',A 33019.821 -1.56641.440 1.00 38.99 A N
ATOM 2010N GLNA 33120.119 0.658 41.551 1.00 37 A C

ATOM 2011CA GlNA 33118.711 0.925 . . . A C
ATOM 2012CB GLNA 33118.396 2.411 41.398 1.00 39.93 ATOM2013CG GLNA 33118.544 2.980 42.792 1.00 39.68 A C

ATOM2014CD GLNA 33117.828 4.296 42.919 1.00 40.86 A C

ATOM2015OE1GLNA 33116.595 4.346 42.590 1.00 - 39.60A 0 ATOM2016NE2GLNA 33118.594 5.381 43.042 1.00 41.35 A N

ATOM2017C GLNA 33118.390 0.468 39.869 1.00 36.76 A C

ATOM2018O GLNA 33117.313 -0.07039.609 1.00 36.99 A O

ATOM2019N TRPA 33219.326 0.680 38.952 1.00 35.39 A N

ATOM2020CA TRPA 33219.101 0.257 37,578 1.00 36.10 A C

ATOM2021CB TRPA 33220.174 0.854 36.661 1.00 34.58 A C

ATOM2022GG TRPA 33219.929 2.318 36.409 1.00 34.06 A C

ATOM2023CD2TRPA 33218.733 2.898 35.877 1.00 32.88 A C

ATOM2024CE2TRPA 33218.921 4.297 35.854 1.00 33.56 A C

ATOM2025CE3TRPA 33217.520 2.370 35.421 1.00 33.38 A C

ATOM2026CD1TRPA 33220.775 3.359 36.673 1.00 33.60 A C

ATOM2027NE1TRPA 33220.175 4.553 36.342 1.00 33.42 A N

ATOM2028CZ2TRPA 33217.936 5.176 35.393 1.00 34.19 A C

ATOM2029CZ3TRPA 33216.541 3.245 34.960 1.00 33.31 A C

ATOM2030CH2TRPA 33216.758 4.633 34.952 1.00 32:26 A C

ATOM2031C TRPA 33219.072 -1.26037.477 1.00 36.09 A C

ATOM2032O TRPA 33218.223 -1.84536.778 1.00 35.40 A O

ATOM2033N THRA 33319.989 -1.90138.196 1.00 36.77 A N

ATOM2034CA THRA 33320.053 -3.35238.191 1.00 37.67 A C

ATOM2035CB THRA 33321.247 -3.84539.023 1.00 39.26 A C

ATOM2036OG1THRA 33322.448 -3.22438.534 1.00 40.96 A O

ATOM2037CG2THRA 33321.376 -5.37138.915 1.00 38.45 A C

ATOM2038C THRA 33318.753 -3.97638.725 1.00 37.47 A C
.

ATOM2039O THRA 33318.192 -4.87138.092 1.00 36.75 A O

ATOM2040N ASPA 33418.263 -3.49539.867 1.00 37.76 A N
I

ATOM2041CA ASPA 33417.031 -4.04940.433 1.00 39.75 A C

ATOM2042CB ASPA 33416.555 -3.25841.662 1.00 41.64 A C

ATOM2043CG ASPA 33417.614 -3.13442.752 1.00 44.89 A C

ATOM2044ODiASPA 33418.483 -4.02942.890 1.00 46.63 A O

ATOM2045OD2ASPA 33417.557 -2.13043.494 1.00 46.87 A O

ATOM2046C ASPA 33415.918 -4.01339.391 1.00 40.01 A C

ATOM2047O ASPA 33415.176 -4.99039.210 1.00 39.16 A O

ATOM2048N ARGA 33515.812 -2.87338.707 1.00 39.92 A N

ATOM2049CA ARGA 33514.782 -2.67237.688 1.00 38.98 A C

ATOM2050CB ARGA 33514.769 -1.19737.256 1.00 37.26 A C

ATOM2051CG ARGA 33514.192 -0.26838.335 1.00 36.06 A C

ATOM2052CD ARGA 33514.537 1.200 38.116 1.00 34.60 A C

ATOM2053NE ARGA 33513.881 2.067 39.099 1.00 34.99 A N

ATOM2054CZ ARGA 33512.598 2.431 39.049 1.00 33.62 A C

ATOM2055NH1ARGA 33511.830 2.010 38.053 1.00 34.02 A N

ATOM2056NH2ARGA 33512.071 3.194 40.003 1.00 30.11 A N

ATOM2057C ARGA 33514.921 -3.59636.479 1.00 37.87 A C

ATOM2055O ARGA 33513.947 -4.22336.065 1.00 38.08 A O

ATOM2059N ILEA 33616.123 -3.69635.922 1.00 38.42 A N

ATOM2060CA ILEA 33616.330 -4.55934.756 1.00 39.05 A C

ATOM2061CB ILEA 33617.752 -4.34434.127 1.00 39.35 A C

ATOM2062CG2ILEA 33618.833 -4.95635.010 1.00 39.36 A C

ATOM2063CG1ILEA 33617.829 -5.00832.751 1.00 39.99 A C

ATOM2064CD1ILEA 33616.777 -4.55931.786 1.00 39.75 A C

ATOM2065C ILEA 33616.132 -6.02535.153 1.00 39.62 A C

ATOM2066O ILEA 33615.510 -6.80734.423 1.00 37.59 A 0 ATOM2067N META 33716.645 -6.39136.326 1:00 41.70 A N

ATOM2068CA META 33716.500 -7.75736.816 1.00 42.64 A C

ATOM2069CB META 33717.284 -7.94038.115 1.00 44.52 A C

ATOM2070CG META 33718.798 -7.95037.907 1.00 47.36 A C

ATOM2071SD META 33719.328 -9.08436.562 1.00 50.44 A S

ATOM2072CE META 33718.906 -10.69037.268 1.00 50.78 A C

ATOM2073C META 33715.023 -8.07037.022 1.00 42.29 A C

ATOM2074O META 33714.540 -9.12636.602 1.00 41.39 A O

ATOM2075N GLUA 33814.305 -7.14337.652 1.0D 42.82 A N
ATOM2076CA GLUA 33812.868 -7.31437.875 1.00 43.48 A C

ATOM2077CB GLUA 33812.267 -6.06038.497 1.00 45.17 A C

ATOM2078GG GLUA 33810.814 -6.22138.897 1.00 48.38 A C

ATOM2079CD GLUA 33810.202 -4.93239.415 1.00 50.90 A C

ATOM2080OE1GLUA 33810.889 -4.20940.187 1.00 51.03 A O

ATOM2081OE2GLUA 3389.038 -4.64839.057 1.00 50.58 A O

ATOM2082C GLUA 33812.190 -7.55936.532 1.00 43.36 A C

ATOM2083O GLUA 33811.403 -8.49336.372 1.00 42.95 A O

ATOM2084N GLUA 33912.509 -6.70835.563 1.00 42.79 A N

ATOM2085CA GLUA 33911.937 -6.82834.231 1.00 42.87 A C

ATOM2086CB GLUA 33912.400 5.649 33.367 1.00 42.47 A C

ATOM2087CG GLUA 33911.657 -5.51532.058 1.00 42.28 A C

ATOM2088CD GLUA 339.11.898 -4.17831.373 1.00 40.59 A C
ATOM2089OE1GLUA 33911.627 -3.12631.991 1.00 36.66 A O

ATOM2090OE2GLUA 33912.354 -4.19430.209 1.00 40.15 A O

ATOM2091C GLUA 33912.342 -8.16633.600 1.00 43.00 A C
ATOM2092O GLUA 33911.533 -8.81232.929 1.00 42.55 A O

ATOM2093N PHEA 34013.589 -8.58333.826 1.00 43.65 A N

ATOM2094CA PHEA 34014.077 -9.85533.287 1.00 45.30 A C

ATOM2095CB PHEA 34015.588 -10.01633.507 1.00 46.01 A C

ATOM2096CG PHEA 34016.438 -9.31832.478 1.00 48.05 A C

ATOM2097CD1PHEA 34015.885 -8.86431.278 1.00 48.11 A C

ATOM2098CD2PHEA 34017.802 -9.13932.694 1.00 47.92 A C

ATOM2099CE1PHEA 34016.680 -8.24530.310 1.00 47.60 A C

ATOM2100CE2PHEA 34018.604 -8.52131.732 1.00 48.01 A C

ATOM2101CZ PHEA 34018.042 -8.07430.538 1.00 47.64 A C

ATOM2102C PHEA 34013.362 -11.02933.940 1.00 46.10 A C

ATOM2103O PHEA 34013.097 -12.03333.285 1.00 45.84 A O

ATOM2104N PHEA 34113.065 -10.90835.233 1.00 47.15 A N

ATOM2105CA PHEA 34112.363 -11.97335.942 1.00 48.63 A C

ATOM2106CB PHEA 34112.406 -11.76731.471 1.00 48.87 A C

ATOM2107CG PHEA 34113.781 -11.92638.083 1.00 47.67 A C

ATOM2108CD1PHEA 34114.678 -12.87037.592 1.00 47.31 A C

ATOM2109CD2PHEA 34114.162 -11.14739.174 1.00 47.56 A C

ATOM2110CE1PHEA 34115.934 -13.03438.180 1.00 48.42 A C

ATOM2111CE2PHEA 34115.414 -11.30239.769 1.00 48.08 A C

ATOM2112CZ PHEA 34116.302 -12.24839.271 1.00 47.74 A C

ATOM2113C PHEA 34110.910 -12.03735.470 1.00 49.41 A C

ATOM2114O PHEA 34110.384 -13.12335.226 1.00 49.39 A 0 ATOM2115N ARGA 34210.262 -10.88135.339 1.00 50.28 A N

ATOM2116CA ARGA 3428.874 -10.85534.878 1.00 51.53 A C

ATOM2117CB ARGA 3428.372 -9.42534.688 1.00 53.75 A C

ATOM2118CG ARGA 3428.172 -8.60235.936 1.00 57.49 A C

ATOM2119CD ARGA 3427.889 -7.18135.490 1.00 62.15 A C

ATOM2120NE ARGA 3427.603 -6.24536.573 1.00 65.35 A N

ATOM2121CZ ARGA 3427.577 -4.92236.413 1.00 66.58 A C

ATOM2122NH1ARGA 3427.829 -4.39435.216 1.00 66.03 A N

ATOM2123NH2ARGA 3427.285 -4.12837.441_1.00 66.70 A N

ATOM2124C ARGA 3428.774 -11.56733.538 1.00 50.96 A C

ATOM2125O ARGA 3427.769 -12.20833.242 1.00 51.50 A O

ATOM2126N GLNA 3439.811 -11.43132.715 1.00 50.52 A N

ATOM2127CA GLNA 3439.811 -12.07731.413 1.00 50.14 A C

ATOM2128CB GLNA 34310.914 -11.52730.512 1.00 48.72 A C

ATOM2129CG GLNA 34310.909 -12.18629.144 1.00 48.00 A C

ATOM2130CD GLNA 34311.829 -11.51328.159 1.00 47.83 A C

ATOM2131OE1GLNA 34311.792 -10.29127.994 1.00 47.60 A O

ATOM2132NE2GLNA 34312.657 -12.30627.484 1.00 46.37 A N

ATOM2133C GLNA 34310.020 -13.56331.612 1.00 51.24 A C

ATOM2134O GLNA 3439.365 -14.38330.963 1.00 50.34 A O

ATOM2135N GLYA 34410.946 -13.90332.507 1.00 51.97 A N

ATOM2136CA GLYA 34411.204 -15.30032.798 1.00 53.55 A C

ATOM2137C GLYA 3449.913 -15.94333.275 1.00 54.29 A C

ATOM2138O GLYA 3449.574 -17.05132.856 1.00 53.33 A O

ATOM2139N ASPA 3459.191 -15.23734.145 1.00 55.50 A N

ATOM2140CA ASP~ 3457.925 -15.73534.671 1.00 58.03 A C
A

ATOM2141CB ASP. 3457.327 -14.75735.686 1.00 57.64 A C
A

ATOM2142CG ASPA 3458.147 -14.65936.960 1.00 58.05 A C

ATOM2143OD1ASPI 3458.957 -15.57537.232 1.00 57.71 A O
A

ATOM2144OD2ASPA 3457.970 -13.66737.698 1.00 57.83 A 0 ATOM2145C ASPA 3456.936 -15.95033.537 1.00 60.09 A C

ATOM2146O ASPA 3456.359 -17.02833.408 1.00 61.16 A O

ATOM2147N ARGA 3466.742 -14.92932.708 1.00 61.96 A N

ATOM2148CA ARGA 3465.820 -15.04831.588 1.00 63.61 A C

ATOM2149CB ARGA 3465.682 -13.70730.861 1.00 63.35 A C

ATOM2150CG ARGA 3464.931 -12.66431.678 1.00 64.15 A C

ATOM2151CD ARGA 3464.262 -11.62130.793 1.00 64.75 A C

ATOM2152NE ARGA 3465.166 -10.56730.333 1.00 64.86 A N

ATOM2153CZ ARGA 3464.841 -9.66329.413 1.00 64.26 A C

ATOM2154NH1ARGA 3463.642 -9.68828.851 1.00 64.63 A N

ATOM2155NH2ARGA 3465.705 -8.72229.065 1.00 64.88 A N

ATOM2156C ARGA 3466.235 -16.15030.615 1.00 64.81 A C

ATOM2157O ARGA 3465.382 -16.87830.110 1.00 65.31 A O

ATOM2158N GLUA 3477.534 -16.28030.354 1.00 66.46 A N

ATOM2159CA GLUA 3478.022 -17.32129.450 1.00 68.28 A C

ATOM2160CB GLUA 3479.545 -17.23229.257 1.00 67.40 A C

ATOM2161CG GLUA 34710.024 -16.03128.450 1.00 67.10 A C

ATOM2162CD GLUA 34711.519 -16.06928.160 1.00 66.24 A C

ATOM2163OE1GLUA 34712.310 -16_25629.105 1_.00_65.71 A O

ATOM2164OE2GLUA 347_ -15_90226.985 1.00_ 66.60 A 0

11.905 ATOM2165C GLUA 3477.676 18.68_530.035 1_.00____70._20A C
ATOM2166O GLUA 3477.144 -19.55229.340 1.00 70.91 A O

ATOM2167N ARGA 3487.982 -18.86131.319 1.00 71.88 A N

ATOM2168CA ARGA 3487.721 -20.10832.033 1.00 73.32 A C

ATOM2169CB ARGA 3488.154 -19.95133.490 1.00 73.82 A C

ATOM2170CG ARGA 3487.800 -21.10834.406 1.00 74.29 A C

ATOM2171CD ARGA 3488.738 -21.11435.602 1.00 74.87 A C

ATOM2172NE ARGA 3488.879 -19.78236.184 1.00 75.05 A N

ATOM2173CZ ARGA 34810.046 -19.22036.485 1.00 75.86 A C

ATOM2174NH1ARGA 34811.180 -19.87336.261 1.00 76.10 A N
ATOM2175NH2ARGA 34810.081 -18.00037.007 1.00 76.42 A N

ATOM2176C ARGA 3486.256 -20.53131.961 1.00 74.46 A C
ATOM2177O ARGA 3485.946 -21.66831.596 1.00 74.53 A O

ATOM2178N GLUA 3495.364 -19.60632.311 1.00 75.33 A N

ATOM2179CA GLUA 3493.925 -19.84732.292 1.00 76.28 A C

ATOM2180CB GLUA 3493.180 -18.52132.459 1.00 76.57 A C

ATOM2181CG GLUA 3493.641 -17.68333.640 1.00 77.58 A C

ATOM2182CD GLUA 3493.071 -16.27133.621 1.00 78.35 A C
ATOM2183OE1GLUA 3493.194 -15.59532.578 1.0D 79.19 A 0 ATOM2184OE2GLUA 3492.507 -15.83234.649 1.00 78.70 A 0 ATOM2185C GLU_A 3493.485 -20.498~ 30.9821.00 77.24 A C

ATOM2186O GLUA 3492.519 -21.25930.949 1.00 77.35 A 0 ATOM2187N ARGA 3504.206 -20.19129.907 1.00 78.46 A N

ATOM2188CA ARGA 3503.893 -20.70828.578 1.00 79.34 A C

ATOM2189CB ARGA 3504.058 -19.58527.548 1.00 80.10 A C

ATOM2190CG ARGA 3503.458 -18.25828.D13 1.00 81.28 A C
ATOM2191CD ARGA 3503.449 -17.19326.925 1.00 81.72 A C
ATOM2192NE ARGA 3503.003 -15.90127.448 1.00 81.81 A N
ATOM2193CZ ARGA 3502.570 -14.89726.692 1.00 82.23 A C

ATOM2194NH1ARGA 3502.520 -15.03325.371 1.00 82.55 A N

ATOM2195NH2ARGA 3502.187 -13.75727.255 1.00 81.59 A N

ATOM2196C ARGA 3504.753 -21.90828.183 1.00 79.45 A C

ATOM2197O ARGA 3504.610 -22.44827.086 1.00 78.91 A O

ATOM2198N GLYA 3515.644 -22.32029.080 1.00 80.03 A N
' ATOM2199CA GLYA 3516.505 -23.45828.801 1.00 81.18 A C

ATOM2200C GLYA 3517.643 -23.13327.851 1.00 81.60 A C

ATOM2201O GLYA 3518.262 -24.02627.268 1.00 81.07 A O

ATOM2202N META 3527.915 -21.84227.692 1.00 82.45 A N

ATOM2203CA META 3528.986 -21.38526.817 1.00 83.18 A C
ATOM2204CB META 3528.748 -19.93426.382 1.00 83.67 A C

ATOM2205CG META 3527.615 -19.73125.390 1.00 84.60 A C

ATOM2206SD META 3527.488 -17.99224.914 1.00 85.45 A S

ATOM2207CE META 3529.056 -17.75924.068 1.00 84.50 A C

ATOM2208C META _ 10.337 -21.471_ _ 83.27 A C
ATOM2209O META 35210.441 -21.28627.511 1.00 82.98 A O
352 28.726 1.00 ATOM2210N GLUA 35311.370 -21.75726.727 1.00 83.33 A N

ATOM_2211CA GLUA 353_12.728 -21.84427.246 1.00 83.54 A C

ATOM2212CB GLUA 35313.699 -22.03026.083 1.00 84.23 A C

ATOM2213CG GLUA 35315.130 -22.32226.475 1.00 85.11 A C

ATOM2214CD GLUA 35315.985 -22.65525.268 1.00 85.85 A C

ATOM2215OE1GLUA 35315.608 -23.58524.523 1.00 85.67 A O

ATOM2216OE2GLUA 35317.025 -21.99225.063 1.00 86.36 A O

ATOM2217C GLUA 35312.997 -20.51927.960 1.00 83.23 A C

ATOM2218O GLUA 35312.777 -19.44927.391 1.00 83.32 A O

ATOM2219N ILEA 35413.455 -20.58629.207 1.00 82.46 A N

ATOM2220CA ILEA 35413.719 -19.37529.977 1.00 81.41 A C

ATOM2221CB ILEA 35413.751 -19.68031.486 1.00 81.49 A C

ATOM2222CG2ILEA 35414.043 -18.40632.265 1.00 81.61 A C

ATOM2223CG1ILEA 35412.404 -20.27331.913 1,00 81.29 A C

ATOM2224CD1ILEA 35412.303 -20.60133.389 1.00 81.40 A C

ATOM2225C ILEA 35415.009 -18.66629.564 1.00 80.50 A C

ATOM2226O ILEA 35416.106 -19.21729.671 1.00 79.99 A O

ATOM2227N SERA 35514.851 -17.42929.096 1.00 79.95 A N

ATOM2228CA SERA 35515.963 -16.59828.636 1.00 79.17 A C

ATOM2229CB SERA 35515.430 -15.25828.114 1.00 78.53 A C

ATOM2230OG SERA 35514.470 -15.44627.085 1.00 77.40 A O

ATOM2231C SERA 35517.007 -16.33729.718 1.00 78.97 A C

ATOM2232O SERA 35516.682 -16.26730.904 1.00 78,74 A O

ATOM2233N PROA 35618.279 -16.18129.315 1.00 78.69 A N

ATOM2234CD PROA 35618.758 -16.21527.921 1.00 78.28 A C

ATOM2235CA PROA 35619.391 -15.92430.237 1.00 78.74 A C

ATOM2236CB PROA 35620.521 -15.52929.296 1.00 78.27 A C

ATOM2237CG PROA 35620.249 -16.37528.099 1.00 78.39 A C

ATOM2238C PROA 35619.081 -14.82831.265 1.00 78.99 A C

ATOM22390 PROA 35618.496 -13.79630.924 1.00 78.98 A 0 ATOM2240N META 35719.479 -15.06632.516 1.00 78.45 A N

ATOM2241CA META 35719.266 -14.12433.615 1.00 78:27 A C

ATOM2242CB META 35719.802 -12.73233.251 1.00 78.65 A C

ATOM2243CG META 35721.287 -12.65232.920 1.00 79.21 A C

ATOM2244SD META 35721.838 -10.93332.629 1.00 80.32 A S

ATOM2245CE META 35721.509 -10.75030.859 1.00 79.33 A C

ATOM2246C META 35717.799 -13.97734.029 1.00 78.13 A C

ATOM22470 MET'A 35717.502 -13.32835.030 1.00 78.30 A O

ATOM2248N CYSA 35816.888 -14.58233.273 1.00 77.91 A N

ATOM2249CA CYSA 35815.459 -14.46333.563 1.00 77.86 A C

ATOM2250CB CYSA 35814.663 -14.57532:259 1.00 77.46 A C

ATOM2251SG CYSA' 35814.942 -13.21831.097 1.00 75.81 A S

ATOM2252C CYSA 35814.843 -15.40434.604 1.00 78.23 A C

ATOM22530 CYSA 35813.736 -15.15135.084 1.00 77.79 A O

ATOM2254N ASPA 35915.538 -16.47834.962 1.00 78.80 A N

ATOM2255CA ASPA 35914.985 -17.41635.937 1.00 79.52 A C

ATOM2256CB ASPA 3_59_15.643 -18.79035.797 1.00 80.05 A C

ATOM2257CG ASPA 35914.748 -19.91136.292 1.00 80.01 A C

ATOM2258OD1ASPA 35914.142 -19.75537.372 1.00 80.25 A O

ATOM2259OD2ASPA 35914.652 -20.94835.602 1.00 80.40 A O

ATOM2260C ASPA 35915.156 -16.92537.371 1.0D 79.70 A C

ATOM2261O ASPA 35916.213 -17.11437.976 1.00 79.90 A O

ATOM2262N LYSA 360t4.107 -16.31537.920 1.00 79.63 A N

ATOM2263CA LYSA 36014.165 -15.79439.282 1.00 79.53 A C

ATOM2264CB LYSA 36012.871 -15.05039.636 1.00 79.08 A C

ATOM2265CG LYSA 36011.638 -15.92439.775 1.00 78.68 A C

ATOM2266CD LYSA 36010.459 -15.09540.278 1.00 78.81 A C

ATOM2267CE LYSA 3609.200 -15.93440.457 1.00 78.35 A C

ATOM2268NZ LYSA 3608.063 -15.10940.955 1.00 78.19 A N

ATOM2269C LYSA 36014.429 -16.88240.315 1.00 79.47 A C

I 2270O LYSA 36014.576 -16.59541 504 1 00 79 A 0 ATOMI I I I ~ I ~ 48 I

ATOM2271N HISA 36114.489 -18.13139.863 1.00 79.31 A N

ATOM2272CA HISA 36114.746 -19.24140.770 1.00 79.40 A C

ATOM2273CB HISA 36113.866 -20.44040.407 1.00 78.48 A C

ATOM2274CG HISA 36112.403 -20.19440.614 1.00 78.35 A C

ATOM2275CD2HISA 36111.330 -20.48539.841 1.00 78.00 A C

ATOM2276ND1HISA 36111.904 -19.59641.753 1.00 77.89 A N

ATOM2277CE1HISA 36110.587 -19.53041.671 9.00 77.90 A C

ATOM2278NE2HISA 36110.213 -20.06340.522 1.00 77.62 A N

ATOM2279C HISA 36116.221 -19.64340.767 1.00 79.60 A C

ATOM2280O HISA 36116.759 -20.04541.800 1.00 79.56 A O

ATOM2281N ASNA 36216.871 -19.52439.611 1.00 79.61 A N

ATOM2282CA ASNA 36218.286 -19.88839.490 1.00 79.37 A C

ATOM2283CB ASNA 36218.498 -20.85738.338 1.00 80.19 A C

ATOM2284CG ASNA 36217.366 -21.87238.217 1.00 81.43 A C

ATOM2285OD1ASNA 36216.733 -22.24039.211 1.00 81.50 A O

ATOM2286ND2ASNA 36217.116 -22.33836.994 1.00 81.23 A N

ATOM2287C ASNA 36219.075 -18_58539.226 1.00 78.90 A C

ATOM2288O ASNA 36219.988 -18.55438.397 1.00 78.66 A 0 ATOM2289N ALAA 36318.711 -17.53439.956 1.00 78.01 A N

ATOM2290CA ALAA 36319.323 -16.21539.829 1.00 77.19 A C

ATOM2291CB ALAA 36318.464 -15.19040.563 1.00 77.43 A C

ATOM2292C ALAA 36320.773 -16.09640.301 1.00 76.60 A C

ATOM2293O ALAA 36321.166 -16.66741.319 1.00 77.00 A O
ATOM2294N SERA 36421.559 -15.33139.551 1.00 75.29 A N

ATOM2295CA SERA 36422.964 -15.09439.868 1.00 74.06 A C

ATOM2296CB SERA 36423.870 -15.95338.976 1.00 74.77 A C

ATOM2297OG SERA 36423.652 -17.33739.187 1.00 76.30 A O

ATOM2298C SERA 36423.252 -13.61639.612 1.00 72.35 A C

ATOM2299O SERA 36424.241 -13.27038.975 1.00 71.96 A 0 ATOM2300N VALA 36522.374 -12.75440.110 1.00 70.53 A N
ATOM2301CA VALA 36522.513 -11.31739.924 1.00 68.79 A C

ATOM2302CB VALA 36521.734 -10.53741.011 1.00 68.74 A C

ATOM2303CGtVALA 36521.893 -9.03640.794 1.00 67.88 A C

ATOM2304CG2VALA 36520.261 -10.92340.975 1.00 68.14 A C

ATOM2305C VALA 36523.965 -10.84739.920 1.00 68.16 A .
ATOM2306O VALA 36524.403 -10.19438.971 1.00 68.21 A C
O

ATOM2307N GLUA 36624.710 -11.18540.972 1.00 66.92 A N
ATOM2308CA GLUA 36626.109 -10.77841.082 1.00 65.71 A C

ATOM2309CB GLUi 36626.714 -11.28842.390 1.00 66.30 A C
ATOM2310CG GLUA 36625.985 -10.82843.644 1.00 66.90 A C
A

ATOM2311CD GLUA 36624.766 -11.67443.960 1.00 67.65 A C

ATOM2312OE1GLUA 36624.050 -11.34944.934 1.00 67.52 A O

ATOM2313OE2GLUA 36624.529 -12.67043.239 1.00 68.26 A O

ATOM2314C GLUA 36626.963 -11.25739.911 1.00 64.94 A C

ATOM2315O GLUA 36627.801 -10.51439.397 1.00 64.13 A O

ATOM2316N LYSA 36726.754 -12.50339.497 1.00 64.02 A N

ATOM2317CA LYSA 36727.506 -13.06738.383 1.00 62.72 A C

ATOM2318CB LYSA 36727.265 -14.57638.290 1.00 64.46 A C

ATOM2319CG LYSA 36727.716 -15.38539.495 1.00 66.18 A C

ATOM2320CD LYSA 36727.389 -16.86039.277 1.00 68.06 A C

ATOM2321CE LYSA 36727.838 -17.73840.439 1.00 68.74 A C

ATOM2322NZ LYSA 36727.397 -19.15740.243 1.00 69.63 A N

ATOM2323C LYSA 36727.097 -12.40437.067 1.00 60.84 A C
ATOM2324O LYSA 36727.943 -12.11136.219 1.00 60.97 A O

ATOM2325N SERA 36825.796 -12.17536.903 1.00 58.73 A N

ATOM2326CA SERA 36825.264 -11.54235.696 1.00 56.40 A C

ATOM2327CB SERA 36823.754 -11.30735.824 1.00 56.76 A C

ATOM2328OG SERA 36823.033 -12.52635.756 1.00 57.68 A O

ATOM2329C SERA 36825.957 -10.21435.435 1.00 54.27 A C

ATOM23300 SERA 36826.490 -9.99034.351 1.00 54.03 A O

ATOM2331N GLNA 36925.943 -9.33736.434 1.00 51.68 A N

ATOM2332CA GLNA 36926.582 -8.03736.309 1.00 48.93 A C

ATOM2333CB GLNA 36926.400 -7.23137.596 1.00 47.51 A C

ATOM2334CG GLNA 36924.960 -6.84037.846 1.00 46.37 A C

ATOM2335CD GLNA 36924.327 -6.20636.622 1.00 46.16 A C

ATOM2336OE1GLNA 36924.865 -5.25136.061 1.00 44.05 A O

ATOM2337NE2GLNA 36923.185 -6.73736.199 1.00 43.56 A N

ATOM2338C GLNA 36928.061 -8.14935.963 1.00 48.00 A C

ATOM2339O GLNA 36928.545 -7.42435.089 1.00 48.15 A O

ATOM2340N VALA 37028.780 -9.05036.632 1.00 46.44 A N

ATOM2341CA VALA 37030.202 -9.22136.342 1.00 45.61 A C

ATOM2342CB VALA 37030.896 -10.22837.286 1.00 45.44 A C

ATOM2343CG1VALA 37032.382 -10.28436.949 1.00 43.47 A C

ATOM2344CG2VALA 37030.691 -9.82638.738 1.00 43.38 A C

ATOM2345C VALA 37030.343 -9.75234.927 1.00 45.59 A C

ATOM2346O VALA 37031.239 -9.34534.185 1.00 44.50 A O

ATOM2347N GLYA 37129.454 -10.67234.565 1.00 45.49 A N

ATOM2348CA GLYA 37129.488 -11.22833.226 1.00 46.88 A C

ATOM2349C GLYA 37129.253 -10.1193?..2201.00 47.33 A C

ATOM2350O GLYA 37129.981 -9.98131.236 1.00 47.64 A O

ATOM2351N PHEA 37228.235 -9.31132.493 1.00 47.59 A N

ATOM2352CA PHEA 37227.863 -8.19231.634 1.00 47.80 A C

ATOM2353CB PHEA 37226.557 -7.57632.147 1.00 49.06 A C

ATOM2354CG PHEA 37226.021 -6.47531.286 1.00 49.69 A C

ATOM2355CD1PHEA 37225.799 -6.67929.928 1.00 50.16 A C

ATOM2356CD2PHEA 37225.712 -5.23631.838 1.00 50 A C
~ ~ ~ ( ~ 41 ATOM 2357CE1PHEA 37225.274 ~~ 29.1311.00 50 A C
-5.664 02 ATOM 2358CE2PHEA 37225.187 _ 31.0521.00 . A C
x,215 50 ATOM 2359CZ PHEA 37224.967 -4.42829.6951.00 . A C
ATOM 2360C PHEA 37228.958 -7.12331.5561.00 50.29 A C
ATOM 2361O PHEA 37229.212 -&,57030.4931.00 47.00 A O
ATOM 2362N ILEA 37329.613 -6.83632.6721.00 47.14 A N

ATOM 2363CA ILEA 37330.660 -5.82732.6641.00 . A C

ATOM 2364CB ILEA 37331.011 5.365 34.0921.00 . A C
ATOM 2365CG2ILEA 37332.212 -4.40334.0511.00 45.27 A C

ATOM 2366CG1ILEA 37329.792 X1.69434.7321.00 . A C
ATOM 2367CD1ILEA 37330.058 -4.08736.1 1.00 44.42 A C
t5 44.84 ATOM 2368C ILEA 37331.955 -6.25731.9701 47 A C

ATOM 2369O ILEA 37332.601 -5.44431.307. . A O
ATOM 2370N ASPA 37432.338 -7.52432,1041.00 47.65 A N
1.00 47 ATOM 2371CA ASPA 37433.583 -7.98631.4$91.00 . A C

ATOM 2372CB ASPA 37434.079 -9.27532.1561 . A C

ATOM 2373CG ASPA 37434,405 -9.08933.624. . A C

ATOM 2374OD1ASPA 37434.706 -7.94534.034. . A O
ATOM 2375OD2ASPA 37434.371 -10.09334.3681.00 48.85 A O
ATOM 2376C ASPA 37433.510 -8.21329.9881.00 48.74 A C
ATOM 2377O ASPA 37434.447 -7.8$429.2641.00 48.24 A O
ATOM 2378N TYRA 37532.404 -8.77129.5141.00 47.98 A N
ATOM 2379CA TYRA 37532.281 -9.04828.0981.00 48.32 A C
ATOM 2380CB TYRA 37531.495 -10.34327,8901.00 49.74 A C
ATOM 2381CG TYRA 37532.152 -11.55228.5111.00 53.96 A C
ATOM 2382CD1TYRA 37531.964 -11.85829.8641.00 58.22 A C
ATOM 2383CE1TYRA 37532.590 -12.96030.4491.00 59.54 A C
ATOM 2384CD2TYRA 37532.985 -12.38127.7531.00 61.49 A C
ATOM 2385CE2TYRA 37533.615 -13.48528.3271.00 59.35 A C
ATOM 2386CZ TYRA 37533.413 -13.76829.6741.00 61.31 A C
ATOM 2387OH TYRA 37534.037 -14.85530.2451.00 62.48 A O
ATOM 2388C TYRA 37531.665 -7.94827.2391.00 64.79 A C
ATOM 2389O TYRA 37531.914 -7.89226.0351.00 48.72 A O
ATOM 2390N ILEA 37630.879 -7.06627.8471.00 48.42 A N
ATOM 2391CA ILEA 37630.221 -6.00827.0861.00 47.35 A C
ATOM 2392CB ILEA 37628.687 -6.19727.1451.00 45.08 A C
ATOM 2393CG2ILEA 37627.975 5.028 26.4691.00 44.98 A C
ATOM 2394CG1ILEA 37628.317 -7.52926.4811.00 44.12 A C
ATOM 2395CD1ILEA 37626.863 -7.91426.6451.00 45.35 A C
ATOM 2396C ILEA 37630.553 x.576 27.4911.00 45.64 A C
ATOM 2397O ILEA 37631.177 -3.84126.7271.00 44.01 A 0 A70M 2398N VALA 37730.137 -4.18628.6931.00 43.28 A N
ATOM 2399CA VALA 37730.340 -2.82829.1711.00 42.78 A C
ATOM 2400CB VALA 37729.684 -2.63130.552t.00 42.02 A C
ATOM 2401CGtVALA 37729.692 -1.17330.9211.00 40.83 A C
ATOM 2402CG2VALA 37728.262 -3.14330.5251.00 39.99 A C
ATOM 2403C VALA 37731.775 -2.31929.2361.00 41.38 A C
ATOM 2404O VALA 37732.068 -1.23628.7301.00 43.27 A O
ATOM 2405N HISA 37832.673 -3.08229.8531.00 43.52 A N
ATOM 2406CA HISA 37834.053 -2.63429.9661.00 43.67 A C
ATOM 2407CB HISA 37834.851 -3.52630.9301.00 43.40 A C
ATOM 2408CG HISA 37836.123 -2.89531.4101.00 43.35 A C
ATOM 2409CD2HISA 37836.431 -2.29532.5861.00 43.09 A C
ATOM 2410ND1HISA 37837.237 -2.75930.6081.00 43.07 A N
ATOM 2411CE1HISA 37838.175 -2.10031.2681.00 42.45 A C
ATOM 2412NE2HISA 37837.710 -1.80832.4711.00 42.78 A N
ATOM 2413C HISA 37834.769 -2.5612$.6221.00 43.84 A C
ATOM 2414O H!SA 37835.464 -1.58428.3371.00 43.37 A O
ATOM 2415'N PROA 37934.620 -3.59327.7781.00 43.39 A N
ATOM 2416CD PROA 37933.918 -4.$8027.9351.00 43.58 A C
ATOM 2417CA PROA 37935.310 -3.51726.4851.00 43.35 A C
ATOM 2418CB PROA 37934.879 -4.$0125.7841.00 44.00 A C
ATOM 2419CG PROA 37934.634 -5.75526.9321.00 44.11 A C
ATOM 2420C PROA 37934.872 -2.26625,7257.00 44.38 A C
ATOM 2421O PROA 37935.679 -1.60625.0671.00 44.76 A O
ATOM 2422N LEUA 38p33.888 -1.93925,8511.00 45.17 A N
ATOM 2423CA LEUA 38032.988 -0.78725.1881.00 44.64 A C
ATOM 2424CB LEUA 38031.469 -0.83325.3411.00 43.19 A C
ATOM 2425CG LEUA 38030.672 0.153 24.4851.00 43.81 A C
ATOM 2426CDTLEUA 38030.895 -0.16723.0131.00 44.01 A C
ATOM 2427CD2LEUA 38029.193 0,057 24.8241.00 45.25 A C
ATOM 2428C LEUA 38033.501 0.544 25.7201.00 44.66 A C
ATOM 2429O LEUA 38033.961 1.396 24.9571.00 42.82 A 0 ATOM 2430N TRPA 38133.413 0.732 27.0311.00 41.07 A N
ATOM 2431CA TRPA 38133.872 1.981 27.6241.00 42.64 A C
ATOM 2432CB TRPA 38133.346 2.113 29.0531.00 42.84 A C
ATOM 2433CG TRPA 38131.925 2.551 29,0811.00 41.22 A C
ATOM 2434CD2TRPA 38131.460 3.900 29.1041.00 40.42 A C
ATOM 2435CE2TRPA 38130.049 3.860 29.0381.00 39.34 A C
ATOM 2436CE3TRPA 38132.099 5.141 29.1671.00 39.37 A C
ATOM 2437CD1TRPA 38130 1.00 38.92 . 1.759 29.0091.00 41.01 A C
ATOM 2438NE1TRPA 3810 2.542 28.9821.00 39.90 A N
ATOM 2439CZ2TRPA 38129.673 5.014 29.0381.00 38.62 A C
ATOM 2440CZ3TRPA 38129..2706.288 29.1661.00 40.94 A C
ATOM 2441CH2TRPA 38131.323 6.215 29.1001.00 39.12 A C
ATOM 2442C TRPA 38129.921 2.158 27.5961.00 43.58 A C
35.384 ATOM2443O TRPA 38135.890 3.284 27.5731.00 42.95 A O

ATOM2444N GLUA 38236.107 1.047 27.5981.00 45.00 A N

ATOM2445CA GLUA 38237.561 1.497 27.5501.00 47.21 A C

ATOM2446CB GLUA 38238.133 -0.31527.7291.00 48.99 A C

ATOM2447CG GLUA 38239.645 -0.39927.8631.00 51.35 A C

ATOM2448CD GLUA 38240.133 -1.83828.0231.00 53.81 A C

ATOM2449OE1GLUA 38240.035 -2.61727.0481.00 54.93 A O

ATOM2450OE2GLUA 38240.602 -2.19529.1261.00 55.14 A O
ATOM2451C GLUA 38237.918 1.660 26.1741.00 46.98 A C

ATOM2452O GLUA 38238.750 2.563 26.0521.00 46.79 A O

ATOM2453N THRA 38337.268 1.127 25.1411.00 46.63 A N

ATOM2454CA THRA 38337.501 1.594 23.7791.00 47.09 A C
ATOM2455CB THRA 38336.724 0.763 22.7531.00 47.20 A C

ATOM2456OG1THRA 38336.953 -0.631_ 22.9871.00 47.92 A O

ATOM2457CG2THRA 38337.179 1.104 21.3531.00 46.06 A C
ATOM2458C THRA 38337.042 3.048 23.6701.00 47.75 A C

ATOM2459O THRA 38337.672 3.861 22.9881.00 48.78 A O

ATOM2460N TRPA 38435.947 3.383 24.3451.00 47.88 A N

ATOM2461CA TRPA 38435.459 4.75 24.3041.00 48.62 A C

ATOM_ CB TRPA 38434.052 _ _ _ 47.22 A C
__ 4.8 24.9041.00 ATOM2463CG TRPA 35433.556 _ 24.881__ 45.83 A C
_ 1.00 6.284 ATOM2464CD2TRPA 38432.870 6.930 23.8011.00 45.41 A C

ATOM2465CE2TRPA 38432.687 8.276 24.1681.00 44.98 A C
ATOM2466CE3TRPA 38432.394 6.495 22.5561.00 45.58 A C

ATOM2467CD1TRPA 38433.749 7.238 25.8341.00 45.14 A C

ATOM2468NE1TRPA 38433.232 8.441 25.4141.00 45.21 A N

ATOM2469CZ2TRPA 38432.046 9.197 23.3361.00 46.29 A C

ATOM2470C23TRPA 38431.756 7.413 21.7291.00 45.50 A C

ATOM2471CH2TRPA 38431.588 8.747 22.124.1.00 45.37 A C

ATOM2472C TRPA 38436.410 5.677 25.0591.00 49.10 A C
ATOM2473O TRPA 38436.619 6.823 24.6671.00 49.11 A O
ATOM2474N ALAA 38536.979 5.171 26.1501.00 50.79 A N

ATOM2475CA ALAA 38537.922 5.951 26.9431.00 52.49 A C

ATOM2476CB ALAA 38538.289 5.202 28.2091.00 52.97 A C

ATOM2477C ALAA 38539.165 6.214 26.0961.00 53.83 A C

ATOM2478O ALAA 38539.798 7.261 26.2081.00 54.27 A O

ATOM2479N ASPA 38639.510 5.256 25.2421.00 55.24 A N

ATOM2480CA ASPA 38640.658 5.417 24.3601.00 56.61 A C

ATOM2481CB ASPA 38640.914 4.134 23.5651.00 59.27 A C

ATOM2482CG ASPA 38641.510 3.027 24.4091.00 62.51 A C

ATOM2483OD1ASPA 38641.642 1.897 23.8861.00 63.81 A O

ATOM2484OD2ASPA 38641.850 3.282 25.5871.00 65.05 A O

ATOM2485C ASPA 38640.387 6.555 23.3781.00 56.17 A C

ATOM2486O ASPA 38641.210 7.457 23.2161.00 56.04 A O

ATOM2487N LEUA 38739.226 6.505 22.7291.00 54.87 A N

ATOM2488CA LEUA 38738.854 7.515 29.7471.00 53.36 A C

ATOM2489CB LEUA 38737.437 7.250 21.2411.00 53.89 A C

ATOM_249_0CG LEUA 38736.972 8.164 20.1061.00 54.19 A C

ATOM2491CD1LEUA 38737.810 7.886 18.8531.00 54.19 A C

ATOM2492CD2LEUA 38735.496 7.929 19.8321.00 54.36 A C

ATOM2493C LEUA 38738.944 8.955 22.2501.00 52.61 A C

ATOM2494O LEUA 38739.474 9.824 21.5661.00 50.61 A O

ATOM2495N VALA 38838.428 9.205 23.4471.00 52.93 A N

ATOM2496CA VALA 38838.432 10.55224.0051.00 54.36 A C

ATOM2497CB VALA 38837.009 10.95024.4431.00 54.62 A C

ATOM2498CG1VALA 38836.060 10.89723.2451.00 54.25 A C

ATOM2499CG2VALA 38836.528 10.01525.5411.00 53.57 A C

ATOM2500C VALA 38839,378 10.73925.1941.00 55.69 A C

ATOM2501O VALA 38839.284 11.73525.9181.00 54.72 A O

ATOM2502N HISA 38940.290 9.786 25.3861.00 57.53 A N

ATOM2503CA HISA 38941.244 9.841 26.4931.00 59.63 A C

ATOM2504CB HISA 38942.320 8.759 26.3091.00 62.12 A C

ATOM2505CG HISA 38943.243 8.613 27.4801.00 65.59 A C

ATOM2506CD2HISA 38943.228 7.749 28.5251.00 66.88 A C

ATOM2507ND1HISA 38944.327 9.441 27.6851.00 66.85 A N

ATOM2508CE1HISA 38944.940 9.094 28.8031.00 67.57 A C

ATOM2509NE2HISA 38944.293 8.070 29.3331.00 67.91 A N

ATOM2510C HISA 38941.887 11.22626.5991.00 59.35 A C

ATOM2511O HISA 38942.218 11.84725.5871.00 58.75 A O

ATOM2512N PROA 39042.093 11.72127.8311.00 59.48 A N

ATOM2513CD PROA 39C42.802 13.00128.0191.00 59.60 A C

ATOM2514CA PROA 39041.788 11.11329.1331.00 59.95 A C

ATOM2515CB PROA 39042.818 11.76330.0341.00 60.27 A C

ATOM2516CG PROA 39042.771 13.18429.5331.00 59.83 A C

ATOM2517C PROA 39040.366 11.38429.6341.00 59.96 A C

ATOM2518O PROA 39039.941 10.83730.6541 59.92 A O
.00 ATOM2519N ASPA 39139.656 12.24628.913_ 60.08 A N
1.00 ATOM2520CA ASPA 39138.286 12.66129.235_ 58.48 A C
1.00 ATOM2521CB ASPA 39137.572 13.07927.9451.00 59.32 A C

ATOM2522CG ASPA 39138.124 14.36927.3491.00 59.62 A C

ATOM2523OD1ASPA 39139.228 14.81227.7341.00 59.59 A 0 ATOM2524OD2ASPA 39137.439 14.93726.4741.00 60.70 A O

ATOM2525C ASPA 39137.387 11.68230.0041.00 57.02 A C

ATOM2526O ASPA 39136.601 12.10230.8531.00 56.05 A O

ATOM2527N ALAA 39237.494 10.38929.7131.00 56.54 A N

ATOM2528CA ALAA 39236.653 9.393 30.3781.00 56.57 A C

ATOM2529CB ALA 39235.963 8.525 29.326 1.00 55.47 A C
A

ATOM2530C ALA 39237.371 8.497 31.389 1.00 56.84 A C
A

ATOM2531O ALA 39237.005 7.337 31.562 1.00 57.11 A O
A

ATOM2532N GLN 39338.389 9.019 32.063 1.00 57.36 A N
A

ATOM2533CA GLN 39339.102 8.203 33.036 1.00 57.06 A C
A

ATOM2534CB GLN 39340.425 8.871 33.425 1.00 57.84 A C
ATOM2535CG A 39341.303 8.016 34.335 1.00 58.23 A C
GLN
A

ATOM2536CD GLN 39341.555 6.622 33.773 1.00 58.73 A C
ATOM2537OE1A 39342.137 6.466 32.700 1.00 58.54 A O
GLN
A

ATOM2538NE2GLN 39341.112 5.600 34.504 1.00 59.08 A N
A

ATOM2539C GLN 39338.254 7.925 34.282 1.00 56.61 A C
A

ATOM2540O GLN 39338.140 6.775 34.707 1.00 56.84 A O
A

ATOM2541N ASP 39437.650 8.962 34.863 1.00 55.91 A N
A

ATOM2542CA ASP 39436.822 8.771 36.055 1.00 55.85 A C
A

ATOM2543CB ASP 39436.274 10.10536.563 1.00 57.82 A C
A

ATOM2544CG ASP 39437.280 10.86337.410 1.00 61.25 A C
A

ATOM2545OD1ASP 39437.970 10.21938.236 1.00 62.75 A O
A

ATOM2546OD2ASP 39437.373 12.10437.265 1.00 61.75 A O
ATOM2547C A 39435.658 7.807 35.833 1.00 55.06 A C
ASP
A

ATOM2548O ASP 39435.324 7.009 36.713 1.00 55.12 A O
A

ATOM2549N ILE 39535.035 7.886 34.661 1.00 53.45 A N
ATOM2550CA A 39533.918 7.007 34.347 1.00 50.78 A C
ATOM2551CB ILE 39533.200 7.464 33.034 1.00 50.10 A C
A
ILE
i A

ATOM2552CG2ILE 39532.234 6.378 32.541 1.00 49.12 A C
~
A

ATOM2553CG1ILE 39532.447 8.776 33.299 1.00 49.24 A C
i A

ATOM2554CD1ILE 39531.805 9.397 32.080 1.00 48.07 A C
A

ATOM2555C ILE 39534.406 5.562 34.227 1.00 49.51 A C
' A

ATOM2556O ILE 39533.735 4.635 34.681 _ 47.68 A 0 A 1.00 ATOM2557N LEU 39635.577 5.374 33.628 1.00 49.18 A N
A

ATOM2558CA LEU 39636.131 4.032 33.472 1.00 49.63 A C
' A

ATOM2559CB LEU 39637.354 4.059 32.550 1.00 49.68 A C
A

ATOM2560CG LEU 39637.952 2.705 32.134 1.00 51.94 A C
A

ATOM2561CD1LEU 39636.854 1.779 31.598 1.00 50.92 A C
A

ATOM2562CD2LEU 39639.040 2.922 31.077 1.00 50.67 A C
ATOM2563C ' 39636.512 3.482 34.847 1.00 49.67 A C
A
LEU
' A

ATOM2564O LEU 39636.314 2.298 35.133 1.00 47.58 A O
.
A

ATOM2565N ASP 39737.039 4.356 35.701 1.00 50.07 A N
A

ATOM2566CA ASP 39737.431 3.958 37.046 1.00 50.74 A C
i A

ATOM2567CB ASP 39738.093 5.122 37.785 1.00 51.41 A C
( A

ATOM2568CG ASP 39739.462 5.460 37.234 1.00 52.81 A C
!
A

ATOM2569OD1ASP 39740.194 4.520 36.848 1.00 53.09 A O
A

ATOM2570OD2ASP 39739.811 6.663 37.203 1.00 53.45 A O
A

ATOM2571C ASP 39736.213 3.493 37.836 1.00 51.18 A C
i A

ATOM2572O ASP 39736.216 2.404 38.431 1.00 51.28 A O
' A

ATOM2573N THR 39835.172 4.324 37.835 1.00 49.54 A N
i A

ATOM2574CA THR 39833.953 4.008 38.556 1.00 48.23 A C
~
A

ATOM2575CB THR 39832.886 5.095 38.347 1.00 47.66 A C
A

ATOM2576OG1THR 39833.448 6.375 38.664 1.00 46.22 A O
A

ATOM2577CG2THR 39831.678 4.841 39.252 1.00 45.35 A C
.
A

ATOM2578C THR 39833.404 2.670 38.097 1.00 48.39 A C
i A

ATOM2579O THR 39832.829 1.923 38.881 1.00 48.58 A O
A

ATOM2580N LEU 39933.589 2:370 36.818 1.00 48.80 A N
A

ATOM2581CA LEU 39933.114 1.110 36.259 1.00 49.47 A C
' A

ATOM2582CB LEU 39933.198 1.139 34.733 1.00 47.57 A C
A

ATOM2583CG LEU 39932.771 -0.15534.048 1.00 46.40 A C
A

ATOM2584CD1LEU 39931.284 -0.40334.283 1.00 46.31 A C
A

ATOM2585CD2LEU 39933.079 -0.06132.569 1.00 47.69 A C
A

ATOM2586C LEU 39933.951 -0.05036.787 1.00 50.15 A C
A

ATOM2587O LEU 39933.412 -1.07337.209 1.00 49.81 A O
A

ATOM2588N GLU 40035.272 0.118 36.744 1.00 51.77 A N
A

ATOM2589CA GLU 40036.202 -0.89937.222 1.00 52.98 A C
A

ATOM2590CB GLU 40037.649 -0.43636.994 1.00 53.62 A C
A

ATOM2591CG GLU 40038.022 -0.32535.507 1.00 55.07 A C
A

ATOM2592CD GLU 40039.336 0.408 35.249 1.00 56.57 A C
A

ATOM2593OE1GLU 40039.680 0.608 34.065 1.00 57.85 A O
A

ATOM2594OE2GLU 40040.027 0.788 36.21 1.00 57.50 A O
A %

ATOM2595C GLU 40035.934 -1.13938.705 1,00 53.49 A C
A

ATOM2596O GLU 40035.933 -2.27639.170 1.00 53.27 A O
A

ATOM2597N ASP 40135.674 -0.06139.437 1.00 54.11 A N
A

ATOM2598CA ASP 40135.395 -0.16040.863 1,00 55.05 A C
A

ATOM2599CB ASP 40135.422 1.238 _41.5051.00 56.49 A C
A

ATOM2600CG ASP 40136.840 1.826 _ 41.5921.00 58.08 A C
A

ATOM2601ODtASP 40137.760 1.323 40.905 1.00 57.90 A O
A

ATOM2602OD2ASP 40137.035 2.805 42.346 1.00 58.91 A 0 A

ATOM2603C ASP 40134.056 -0.84741.135 1.00 54.41 A C
A

ATOM2604O ASP 40133.930 -1.59342.100 1.00 54.55 A O
A

ATOM2605N ASN 40233.055 -0.61640.289 1.00 54.27 A N
A

ATOM2606CA ASN 40231.760 -1.25540.512 1.00 _ A C
A 4.15 ATOM2607CB ASN 40230:658 -0.59039.675 1.00 _ A C
A 54.11 ATOM2608CG ASN 40230.298 0.800 40.181 1.00 _ A C
A 53.48 ATOM2609OD1ASN 40230.228 1.034 41.385 1.00 53.18 A O
A

ATOM2610ND2ASN 40230.051 1.721 39.261 1.00 53.92 A N
A

ATOM2611C ASN 40231.830 -2.74640.206 1.00 53.88 A C
A

ATOM2612O ASN 402__31.007 -0.53040.689 1.00 51.64 A O
A

ATOM2613N ARG 40332.818 -3.13439.402 1.00 55.29 A N
A

I 2614CA ARG 40333.001 -4.54339 059 1 56 A C
ATOMI I I I I ~ ~ 00 86 I A
I

ATOM2615CB ARG A 40334.003 -4.71637.920 1.00 57.52 A C

ATOM2616CG ARG A 40334.283 -6.18337,645 1.00 59.00 A C

ATOM2617CD ARG A 40335.482 -6.40136.761 1.00 59.95 A C

ATOM2618NE ARG A 40335.671 -7.82336.484 1.00 60.45 A N

ATOM2619CZ ARG A 40336.048 -8.72737.385 1.00 60.49 A C

ATOM2620NH1ARG A 40336.289 -8.36638.640 1.00 59.80 A N

ATOM2621NH2ARG A 4D336.169 -10.00037.030 1.00 59.86 A N

ATOM2622C ARG A 40333.525 -5.29740.281 1.00 57.09 A C

ATOM2623O ARG A 40332.998 -6.34540.648 1.00 56.49 A O

ATOM2624N GLU A 40434.575 -4.76040.898 1.00 58.10 A N
!

ATOM2625CA GLU A 40435.146 -5.38042.084 1.00 59.73 A C

ATOM2626CB GLU A 40436.208 -4.48342.729 1.0D 61.30 A C

ATOM2627CG GLU A 40437.427 -4.19641.865 1.00 65.17 A C

ATOM2628CD GLU A 40438.106 -5.46041.348 1.00 67.71 A C

ATOM2629OE1GLU A 40437.530 -6.12840.456 1.00 68.11 A 0 ATOM2630OE2GLU A 40439.216 -5.78741.836 1.00 69.49 A O

ATOM2631C GLU A 404__ -5.56543.062 1.00 59.81 A C
34.005 ATOM2632O GLU A 40433.674 -6.68943.434 1.0D 60.37 A O

ATOM2633N TRP A 40533.394 -4.45043.457 1.00 59.43 A N

ATOM2634CA TRP A 40532.290 -4.47944.406 1.00 59.13 A C

ATOM2635CB TRP A 40531.486 -3.17644,359 1.00 57.67 A C

ATOM2636CG TRP A 40530.435 -3.13745.419 1.00 55.98 A C

ATOM2637CD2TRP A 405_ -3.60945.306 1.00 55.02 A C
29.085 ATOM2638CE2TRP A 40525.491 -3.48546.583 1.00 54.30 A C

ATOM2639CE3TRP A 40525.323 -4.13044.250 1.00 53.88 A C

ATOM2640CD1TRP A 40530.596 -2.75046.722 1,00 54.72 A C

ATOM2641NEtTRP A 40529.434 -2.95847.426 1.00 53.68 A N

ATOM2642CZ2TRP A 40527.163 -3.86546.835 1.00 54.12 A C

ATOM2643CZ3TRP A 40527.002 -4.51044.500 1.00 54.33 A C

ATOM2644CH2TRP A 40526.438 -4.37645.784 1.00 54.38 A C

ATOM2645C TRP A 40531.355 -5.65544.152 1.00 59.43 A C

ATOM2646O TRP A 40530.964 -6.35445.080 1.00 59.71 A O

ATOM2647N TYR A 40630.996 -5.88042.897 1.00 60.26 A N

ATOM2648CA TYR A 40630.105 -6.98642.592 1.00 61.98 A C

ATOM2649CB TYR A 40629.528 -6.83141.186 1.00 60.48 A C

ATOM2650CG TYR A 40628.130 -6_26_341.182 1.00 59.05 A C

ATOM2651CD1TYR A 40627.070 -6.97241.748 1.00 58:48 A C

ATOM2652CE1TYR A 40625.777 -6.46541.736 1.00 57.81 A C

ATOM2653CD2TYR A 40627.859 -5.02540.603 1.00 58.21 A C

ATOM2654CE2TYR A 40626.567 -4.50940.586 1.00 57.34 A C

ATOM2655CZ TYR A 40625.534 -5.23441.151 1.00 57.47 A C

ATOM2656OH TYR A 40624.255 -4.73441.116 1.00 57.72 A O

ATOM2657C TYR A 40630.783 -8.34542.749 1.00 64.10 A C

ATOM2658O TYR A 40630.110 -9.35042.994 1.00 63.47 A 0 ATOM2659N GLN A 40732.109 -5.37742.609 1.00 66.62 A N

ATOM2660CA GLN A 40732.861 -9.62242.771 1.00 69.29 A C

ATOM2661CB GLN A 40734.342 -9.41242.452 1.00 69.54 A C

ATOM2662CG GLN A 40734.765 -9.95541.100 1.00 70.75 A C

ATOM2663CD GLN A 40734.577 -11.46140.987 1.00 70.95 A C

ATOM2664OE1GLN A 40735.209 -12.23241.710 1.0D 70.34 A O

ATOM2665NE2GLN A 40733.703 -11.88640.075 1.00 70.73 A N

ATOM2666C GLN A 40732.710 -10.07944.217 1.00 70.73 A C

ATOM2667O GLN A 40732.451 -11.25244.489 1.00 71.09 A O

ATOM2668N SER A 40832.873 -9.13745.140 1.00 72.24 A N

ATOM2669CA SER A 40832.730 -9.426_46.5601.00 73.90 A C

ATOM2670CB SER A 40832.815 -8.13547.375 1.00 73.88 A C

ATOM2671OG SER A 40833.925 -7.34546.983 1.00 74.35 A O

ATOM2672C SER A 40831.358 -10.05346.765 1.00 75.24 A C

ATOM2673O SER A 40831.242 -11.22547.116 1.00 75.22 A O

ATOM2674N THR A 40930.325 -9.25446.522 1.00 77.28 A N

ATOM2675CA THR A 40928.935 -9.67546.673 1.00 80.00 A C

ATOM2676CB THR A 40927.992 -8.74545.874 1.00 80.23 A C

ATOM2677OG1THR A 40928.309 -7.38246.170 1.00 80.92 A O

ATOM2678CG2THR A 40926.531 -9.00946.243 1.00 80.22 A C

ATOM2679C THR A 40928.674 -11.11346.232 1.00 81.74 A C

ATOM26800 THR A 40927.757 -11.75946.738 1.00 81,72 A O

ATOM2681N ILE A 41029.473 -11.61045.290 1.00 84.11 A N

ATOM2682CA ILE A 41029.309 -12.97244.786 1.00 86.31 A C

ATOM2683CB ILE A 41030.351 -13.29943.686 1.00 86.09 A C

ATOM2684CG2ILE A 41030.216 -14.75743.251 1.00 86.15 A C

ATOM2685CG1ILE A 41030.150 -12.36842.489 1.00 85.92 A C

ATOM2686CD1ILE A 41031.077 -12.64641.326 1.00 86.04 A C

ATOM2687C ILE A 41029.436 -14.01345.897 1.00 88_.03A C

ATOM2688O ILE A 41030.540 -14.29846.368 1.00 87.97 A 0 ATOM2689N PRO A 41128.301 -14.59946.326 1.0D 89.86 A N

ATOM2690CD PRO A 41126.927 -14.39445.826 1.00 90.18 A C

ATOM2691CA PRO A 41128.324 -15.61047.388 1.00 91.18 A C

ATOM2692CB PRO A 41126.839 -15.85647.661 1.00 90.76 A C

ATOM2693CG PRO A 41126.212 -15.63246.322 1.00 90.51 A C

ATOM2694C PRO A 41129.070 -16.87046.947 1.00 92.29 A C

ATOM2695O PRO A 41128.823 -17.40445.863 1.00 92.36 A O

ATOM2696N GLN A 41229.989 -17.33047.792 1.00 93.69 A N

ATOM2697CA GLN A 41230.786 -18.51747.494 1.00 95.08 A C

ATOM2698CB GLN A 41232.274 -18.14447.426 1.00 95.66 A C

ATOM2699.CG GLN A 41232.602 -17.04446.417 1.00 96.55 A C

ATOM2700CD GLN A 41234.076 -16.65946.413 1.00 97.09 A C

ATOM2701OE1GLNA 41234.938 -17.43845.9961.00 96.77 A O

ATOM2702NE2GLNA 41234.370 -15.45046.8821.00 97.21 A N

ATOM2703C GLNA 41230.570 -19.61348.5411.00 95.61 A C

ATOM2704O GLNA 41231.526 -19.90949.2941.0D 95.91 A O

ATOM2705OXTGLNA 41229.446 -20.16248.6001.00 95.78 A O

ATOM2706CB THRB 86 -10.881-27.141-25.7481.00 100.00B C

ATOM2707OG1THRB 86 -11.741-26.403-26.6271.00 100.00B O

ATOM2708CG2THRB 86 -11.685-27.603-24.5341.00 100.00B C

ATOM2709C THRB 86 -8.920 -25.802-26.5521.00 100.00B C

ATOM2710O THRB 86 -8.187 -26.592-27.1531.00 100.00B O

ATOM2711N THRB 86 -10.166-25.084-24.4951.00 100.00B N

ATOM2712CA THRB 86 -9.692 -26.247-25.3051.00 100.00B C

ATOM2713N GLUB 87 -9.091 -24.538-26.9361.00 100.00B N

ATOM2714CA GLUB 87 -8.414 -23.978-28.1081.0D 100.00B C

ATOM2715CB GLUB 87 -9.274 -22.880-28.7481.00 100.00B C

ATOM2716CG GLUB 87 -9.669 -21.759-27.7821.00 100.00B C

ATOM2717CD GLUB 87 -10.084-20.478-28.4891.00 100.00B C

ATOM2718OE1GLUB 87 -9.214 -19.832-29.1171.00 100.00B O

ATOM2719OE2GLUB 87 -11.279-20.120-28.4161.00 100.00B O

ATOM2720C GLUB 87 -7.050 -23.393-27.7341.00 100.00B C

ATOM2721O GLUB 87 -6.024 -23.751-28.3191.00 100.00B O

ATOM2722N GLNB 88 -7.055 -22.485-26.7611.00 100.00B N

ATOM2723CA GLNB 88 -5.837 -21.838-26.2901.00 100.00B C

ATOM2724CB GLNB 88 -6.137 -20.389-25.8901.00 100.00B C

ATOM2725CG GLNB 88 -6.642 -19.529-27.0451.00 100.00B C

ATOM2726CD GLNB 88 -7.115 -18.152-26.6041.00 100.00B C

ATOM2727OE1GLNB 88 -6.351 -17.372-26.0291.00 100.00B O

ATOM2728NE2GLNB 88 -8.382 -17.847-26.8751.00 100.00B N

ATOM2729C GLNi 8S -5.289 -22.610-25.0971.00 99.85 B C
B

ATOM2730O GLN! 8S -4.174 -22.364-24.6391.00 99.94 B O
B

ATOM2731N GLUB 89 -6.087 -23.553-24.6061.00 99.60 B N

ATOM2732CA GLU' 89 -5.702 -24.378-23.4711.00 99.30 B C
B

ATOM2733CB GLU8 89 -6.933 -25.081-22.9051.00 99.35 B C

ATOM2734CG GLUB 89 -6.653 -25.950-21.7031.00 99.53 B C

ATOM2735CD GLUB 89 -7.926 -26.427-21.0431.00 100.00B C

ATOM2736OE1GLUB 89 -8.810 -26.941-21.7631.00 100.00B O

ATOM2737OE2GLUB 89 -8.042 -26.290-19.8071.00 100.00B O

ATOM2738C GLUB 89 -4.644 -25.401-23.8761.00 99.03 B C

ATOM2739O GLUB 89 -3.626 -25.549-23.1971.00 99.03 B O

ATOM2740N ASPB 90 -4.883 -26.110-24.9781.00 98.49 B N

ATOM2741CA ASPB 90 -3.914 -27.091-25.4571.00 97.69 B C

ATOM2742CB ASPB 9D -4.382 -27.749-26.7651.00 97.86 B C

ATOM2743CG ASPB 90 -5.604 -25.638-26.5801.00 98.10 B C

ATOM2744OD1ASPB 90 -5.571 -29.532-25.7061.00 87.94 B p ATOM2745OD2ASPB 90 -6.596 -28.451-2%.3191.00 97.86 B O

ATOM2746C ASPB 90 -2.618 -26.334-25.7131.00 96.81 B C

ATOM2747O ASPB 90 -1.529 -26.825-25.4241.00 96.72 B O

ATOM2748N VALB 91 -2.763 -25.125-26.2491.00 95.91 B N

ATOM2749CA VALB 91 -1.632 -24.258-26.5691.00 94.89 B C

ATOM2750CB VALB 91 -2.094 -22.994-27.3251.00 94.61 B C

ATOM2751CG1VALB 91 -0.884 -22.187-27 1 94 B C

ATOM2752CG2VALB 91 -2.955 -23.384. . . B

. . . C
ATOM2753C VALB 91 -0.869 -23.809-25 1 94 B C

ATOM2754O VALB 91 0.343 -23.592. . . B O

ATOM2755N LEUB 92 -1. -23.664. . . B N
580 -24.2121.00 93 ATOM2756CA LEUB 92 _ -23.235-22 1 . B
-0.959 962 00 92 . . . C
ATOM2757CB LEUB 92 -2.020 -22.699-21 1 92 B C

ATOM2758CG LEUB 92 -1.552 -21 . . .

. . . 92.59 B C
ATOM2759CD1LEUB 92 -2.739 -21 -20 1 . . . 91.80 B C

. . - 1.00 92.74 B C
ATOM2761C LEUB 92 -0 -24 .

. . - 1.00 92.30 B C
ATOM2762O LEUB 92 0.870 -24.218. 1 92 B

. , . O
ATOM2763N ALAB 93 -0.790 -25.589-22 1 91 B

. . . N
ATOM2764CA ALAB 93 -0.158 -26 -21 1 9 . . . 0.88 B C

. . . 1.00 90.82 B C

. -26.979-22.5371.00 90.24 B C

ATOM2767O ALAB 93 2.221 -27.102-21.8781.00 90.15 B O

ATOM2768N LYSB 94 1.168 -27.005-23.8661 89 B N

ATOM2769CA LYSB 94 2.385 -27.187-24 . . B

. . . C
ATOM2770CB LYSB 94 2.079 -27.037-26 1 88 B

. . . C
ATOM2771CG LYS8 94 1.169 -28 -26 1 . . . 88.61 B C
ATOM2772CD LYSB 94 0.644 -27 -28 1 . . . 88.38 B C
ATOM2773CE LYSB 94 -0.394 -28 -28 1 , . . 87.95 B C

. . - 1.00 87.53 B N
ATOM2775C LYSB 94 3.441 -26.178. 1 88 B

. . . C
ATOM2776O LYSB 94 4.594 -26.538-23 1 88 B

. . . O
ATOM2777N GLUB 95 3.037 -24 -24 1 . . . 88.04 B N
ATOM2778CA GLUB 95 3.951 -23.854-23 1 8 . , 7.71 B C
ATOM2779CB GLUB 95 3.219 -22 -23 1 . . . 87.92 B C

. , . 1.00 88.06 B C

. . -25.7191.00 88.23 B C
AT
M

O 2782OE1GLUB 95 5.120 -20.808-25.1001 87 B O

ATOM2783OE2GLUB 95 4.482 -21.919-26 . .

. . 88.32 B O
ATOM2784C GLUB 95 4.596 -24 -22 . . 1.00 86.95 B C

. - -22.0671.00 86.84 B O
A .6 TOM 2786N LEU8 96 3.877 -24 -21 1 . . . 86.10 B N

ATOM 2787CA LEUB 96 4.403 -25.114-20.1111.00 85.73 B C

ATOM 2788CB LEUB 96 3.261 -25.443-19.1441.00 85.52 B C

ATOM 2789CG LEUB 96 2.409 -24.258-18.6711.00 85.74 B C

ATOM 2790CD1LEUB 96 1.258 -24.753-17.8091.00 85.38 B C

ATOM 2791CD2LEUB 96 3.276 -23.287-17.8841.00 85.22 B C

ATOM 2792C LEUB 96 5.407 -26.265-20.1521.00 85.61 B C

ATOM 2793O LEUB 96 6.140 -26.491-19.1891.00 85.11 B O

ATOM 2794N GLUB 97 5.446 -26.991-21.2661.00 85.64 B N

ATOM 2795CA GLU. 97 6.388 -28.098-21.3991.00 85.55 B C
B

ATOM 2796CB GLUB 97 6.259 -25.773-22.7721.00 85.87 B C

ATOM 2797CG GLUB 97 4.932 -29.478-23.0371.00 86.50 B C

ATOM 2798CD GLUB 97 4.965 -30.328-24.3071.00 86.66 B C

ATOM 2799OE1GLUB 97 5.703 -31.339. -24.3311.00 86.37 B O

ATOM 2800OE2GLUB 97 4.261 -29.982-25.2831.0D 86.37 B O

ATOM 2801C GLU8 97 7.809 -27.559-21.2391.00 85.12 B C

ATOM 2802O GLUB 97 8.748 -28.319-21.0131.00 85.04 B O

ATOM 2803N ASPB 98 7.956 -26.242-21.3611.00 84.55 B N

ATOM 2804CA ASPB 98 9.259 -25.595-21.2321.00 83.76 B C

ATOM 2805CB ASPB 98 9.394 -24.461-22.2571.00 84.40 B C

ATOM 2806CG ASPB 98 9.279 -24.944-23.6891.00 84.62 B C

ATOM 2807OD1ASPB 98 10.009 -25.886-24.0631.00 85.06 B O

ATOM 2808OD2ASPB 98 8.463 -24.373-24.4451.00 84.87 B O

ATOM 2809C ASPB 98 9.485 -25.026-19.8281.00 52.58 B C

ATOM 2810O ASPB 98 10.383 -24.205-19.6221.00 82.76 B O

ATOM 2811N VALB 99 8.678 -25.464-18.8671.00 80.63 B N

ATOM 2812CA VALB 99 8,786 -24.978-17.4941.00 79.16 B C

ATOM 2813CB VALB 99 7.807 -25.729-16.5671.00 79.31 B C

ATOM 2814CG1VALB 99 8.295 -25.673-15.1231.00 79.85 8 C

ATOM 2815CG2VALB 99 6.430 -25.095-16.6661.00 79.38 B C

ATOM 2816C VALB 99 10.185 -25.032-16.8811.00 77.79 B C

ATOM 2817O VALB 99 10.631 -24.066-16.2651.00 77.31 B O

ATOM 2818N ASNB 10010.870 -26.157-17.0321.00 76.27 B N

ATOM 2819CA ASNB 10012.208 -26.295-16.4731.00 75.24 B C

ATOM 2820CB ASNB 10012.500 -27.760-16.1551.0D 75.66 B C

ATOM 2821CG ASNB 10012.223 -28.101-14.7051.00 76.28 B C

ATOM 2822OD1ASN8 10013.038 -27.818-13.8201.00 76.23 B O

ATOM 2823ND2ASNB 10011.061 -28.695-14.4491.00 75.95 B N

ATOM 2824C ASNB 10D13.261 -25.748-17.4171.00 74.41 B C

ATOM 28250 ASNB 10014.455 -25.997-17.2471.00 73.54 B O

ATOM 2826N LYSB 10112.803 -24.993-18.4101.00 73.48 B N

ATOM 2827CA LYSB 10113.692 -24.400-19.3941.00 72.97 B C

ATOM 2828CB LYSB 10113.157 -24.662-20.8061.00 73.75 B C

ATOM 2829CG LYSB 10113.070 -26.139-21.1771.00 74.08 B C

ATOM 2830CD LYSB 10112.526 -26.318-22.5871.00 74.64 B C

ATOM 2831CE LYSB 10112.367 -27.790-22.9501.00 75.39 B C

ATOM 2832NZ LYSB 10111.794 -27.972-24.3171.00 74.84 B N

ATOM 2833C LYSB 10113_853 -22,896-19.1571.00 72.31 B C
~

ATOM 2834O LYSB 10112.884 -22.183-15.8771.00 71.81 B O

ATOM 2835N TRPB 10215.089 -22.427-19.2721.00 70.95 B N

ATOM 2836CA TRPB 10215.407 -21.024-19.0691.00 70.30 B C

ATOM 2837CB TRPB 10216.870 -20.896-18.6521.00 70.29 B C

ATOM 2838CG TRPB 10217.321 -19.505-18.3451.00 69.54 B C

ATOM 2839CD2TRPB 10217.397 -18.900-17.0501.00 69.06 B C
ATOM 2840CE2TRPB 10217.920 -17.602-17.2271.00 68.98 B C
ATOM 2841CE3TRPB 10217.076 -19.331-15.7551.00 68.83 B C

ATOM 2842CD1TRPB 10217.779 -18.576-19.2301.00 69.34 B C
ATOM 2843NE1TRPB 10218.144 -17.430-18.5671.00 69.22 B N
ATOM 2844CZ2TRPB 10218.132 -16.728-16.1561.00 68.86 B C
ATOM 2845CZ3TRPB 10217.286 -18.462-14.6881.00 68.87 B C
ATOM 2846CH2TRPB 10217.810 -17.175-14.8951.00 68,99 B C
ATOM 2847C TRPB 10215.147 -20.194-20.3191.00 70.12 B C
ATOM 2848O TRPB 10215.991 -20.116-21.2081.00 70.49 B O
ATOM 2849N GLYB 10313.975 -19.571-20.3771.00 69.51 B N
ATOM 2850CA GLYB 10313.630 -18.750-21.5201.00 69.09 B C
ATOM 2851C GLYB 10312.151 -18.851-21.8141.00 69.47 B C
ATOM 28520 GLYB 10311.690 -18.438-22.8791.00 69.11 B O
ATOM 2853N LEUB 10411.407 -19.400-20.8571.00 69.88 B N
ATOM 2854CA LEUB 1049.966 -19,580-20.9981.00 70.65 B C
ATOM 2855CB LEUB 1049.341 -19.890-19.6341.00 70.31 B C
ATOM 2856CG LEUB 1047.872 -20.325-19.6091.00 70.64 B C
ATOM 2857CD1LEUB 1047.682 -21.569-20.4521.00 71.14 B C
ATOM 2858CD2LEUB 1047.447 -20.604-18.1781.00 70.09 B C
ATOM 2859C LEUB 1049.284 -18.361-21.6131.00 71.24 B C
ATOM 2860O LEUB 1049.634 -17.219-21.3111.00 71.70 B 0 ATOM 2861N HISB 1058.317 -18.620-22.4891.00 71,58 B N
ATOM 2862CA HISB 1057.558 -17.568-23.1571.00 71.67 B C
ATOM 2863CB HISB 1056.880 -18.143-24.4031.00 73.12 B C
ATOM 2864CG HISB 1057.837 -18.756-25.3861.00 74.54 B C
ATOM 2865CD2HISB 1059.149 -18.514-25.6261.00 74.66 B C
ATOM 2866ND1HISB 1057.459 -19.731-26.2851.00 74.58 B N
ATOM 2867CE1HISB 1058.495 -20.062-27.0351.00 74.98 B C
ATOM 2868NE2HIS8 1059.533 -19.338-26.6561.00 74.79 B N
ATOM 2869C HISB 1056.518 -17.078-22.1551.00 71.15 B C
ATOM 2870O HISB 1055.322 -17.029-22.4421.00 70.55 B O
ATOM 2871N VALB 1067.010 -16,723-20.9721.00 7D.78 B N
ATOM 2872CA VALB 1066.196 -16.254-19.8551.00 70.01 B C

ATOM 2873CB VALB 1067.086 -15.582-18.7751.00 70.37 B C

ATOM 2874CG1VALB 1067.752 -14.333-19.3421.0D 70.10 B C

ATOM 2875CG2VALB 1066.256 -15.247-17.5461.00 69.92 B C

ATOM 2876C VALB 1065.075 -15.296-20.2401.00 69.36 B C

ATOM 28770 VALB 1064.006 -15.304-19.6281.00 68.97 8 O

ATOM 2878N PHEB 1075.307 -14.468-21.2491.00 68.74 B N

ATOM 2879CA PHEB 1074.278 -13.531-21.6621.00 68.45 B C

ATOM 2880CB PHEB 1074.883 -12.465-22.5801.00 67.06 B C

ATOM 2881CG PHE8 1075.807 -11.509-21.8631.00 65.96 B C

ATOM 2882CD1PHEB 1075.341 -10.738-20.7971.00 65.07 B C

ATOM 2883CD2PHEB 1077.136 -11.381-22.2431 64 B C

ATOM 2884CE1PHEB 1076.187 -9.854-20.124. . B C
1.00 63.95 ATOM 2885CE2PHEB 1077.989 -10.498-21.5731.00 64.36 B C

ATOM 2886CZ PHEB 1077.510 -9.734-20.5121.00 63.48 B C

ATOM 2887C PHEB 1073.079 -14.229-22.3121.00 69.24 B C

ATOM 2888O PHEB 1071.939 -13.841-22.0641,00 69.03 B O

ATOM 2889N ARGB 1083.322 -15.261-23.1231.00 70.31 B N

ATOM 2890CA ARGB 1082.221 -15.995-23.7571.00 71.24 B C

ATOM 2891CB ARGB 1082.736 -17.142-24.6291.00 72.96 B C

ATOM 2892CG ARG8 1083.518 -16.750-25.8641.00 75.17 B C

ATOM 2893CD ARGB 1084.006 -18.012-26.5761.00 76.64 B C

ATOM 2894NE ARGB 1084.889 -17.716-27.6991.00 77.70 B N

ATOM 2895CZ ARGB 1084.487 -17.175-28.8421.00 78.42 B C

ATOM 2896NH1ARGB 1083.206 -16.872-29.0201.00 78.86 B N

ATOM 2897NH2ARGB 1085.368 -16.929-29.8051.00 78.81 B N

ATOM 2898C ARGB 1081.370 -16.603-22.6531.00 71.12 B C

ATOM 2899O ARGB 1080.141 -16.562-22.6921.00 71 B O

ATOM 2900N ILEB tOg2.051 -17.181-21.6721.00 . B N
70.99 ATOM 2901CA ILEB 1091.405 -17.812-20.5341.00 71.10 B C

ATOM 2902CB ILEB 1092.457 -18.411-19.5881.00 70.81 B C

ATOM 2903CG2ILEB 109t.78p -19.070-18.4011.00 70.33 B C

ATOM 2904CG1ILEB 1093.324 -19.406-20.3631.00 71.05 B C

ATOM 2905CD1ILEB 1094.436 -20.018-19.5521.00 72.67 B C

ATOM 2906C ILEB 1090.556 -16.805-19.7721.00 71.44 B C

ATOM 2907O ILEB 109-0.368 -17.179-19.0561.00 71.77 B O

ATOM 2908N ALAB 1100.878 -15.525-19.9271.00 71.75 g N

ATOM 2909CA ALA, 1100.133 -14.465-19.2601.00 72.26 B C
B

ATOM 2910CB ALA' 1100.926 -13.158-19.2981.00 72 B C

ATOM 2911C ALAB 110-1.215 -14.285-19.9531.00 . B C
72.53 ATOM 2912O ALAB 110-2.247 -14.129-19.3021.00 72 B O

ATOM 2913N GLUB 111-1.195 -14.314-21.2811.00 . B N
72.48 ATOM 2914CA GLUB 111-2.411 -14.161-22.0691.00 72.86 B C

ATOM 2915CB GLUB 111-2.053 -13.891-23.5331.00 73 B C

ATOM 2916CG GLUB 111-0.768 -13.101-23.7181.00 . B C
74.52 ATOM 2917CD GLUB 111-0.330 -13.022-25.1711.00 75 B C

ATOM 2918OEtGLUB 111-0.447 -14.046-25.8811 . B

. . O
ATOM 2919OE2GLUB 1110.143 -11.943-25 1 76 B

. . . 0 ATOM 2920C GLUB 111-3.232 -15.447-21 1 72 B C

ATOM 2921O GLUB 111-4.340 -15.453. . . B O
-21.4351.00 72 ATOM 2922N LEUB 112-2.665 -16.534-22.4881 . B N

ATOM 2923CA LEUB 112-3.307 -17.847-22.491. . B C
1.00 72 ATOM 2924CB LEUB 112-2.307 -18.916-22.9491.00 . B C
72.61 ATOM 2925CG LEUB 112-1.673 -18.760-24.3371.00 72 B C

ATOM 2926CD1LEUB 112-0.632 -19.844-24.5541.00 . B C
72.08 ATOM 2927CD2LEUB 112-2.747 -18.830-25.4101 72 B C

ATOM 2928C LEUB 112-3.887 -18.253-21.137. . B C
1.00 72 ATOM 2929O LEUB 112-4.895 -18.957-21.0761.00 . B 0 ATOM 2930N SERB 113-3.254 -17.809-20.0561.00 . B N

ATOM 2931CA SERB 113-3.706 -18.152-18.7131.00 . B C

ATOM 2932CB SERB 113-2.514 -18.174-17.7591 . B

. . C
ATOM 2933OG SERB 113-2.919 -18 -16 1 . . . 72.83 B O
ATOM 2934C SERB 113-4.768 -17 -18 . . 1.00 72.48 B C
ATOM 2935O SERB 113-5.329 -17.454-17 1 . , 72.07 B O
ATOM 2936N GLYB 114-5.050 -16 -18 . . 1.00 72.64 B N
ATOM 2937CA GLYB 114-6.026 -15 -18 . . 1.00 72.89 B C

. - -17.3941.00 73.21 B C
ATOM 2939O GLYB 114 .

-5.939 -13.993-16.3341.00 73.02 B O

ATOM 2940N ASNB 115-4.168 -13.801-17 1 73 B

. . . N
ATOM 2941CA ASNB 115-3.416 -12 -16 . . 1.00 73.03 B C
ATOM 2942CB ASNB 115-4.166 -11 -16 . . 1.00 73.62 B C

. . -15.8091.00 74.21 B C

- -10.273 -16.0951.00 73.06 B O
.239 ATOM 2945ND2ASNB 115-4.045 -10.088-14 1 73 . . . B N
ATOM 2946C ASNB 115-3.174 -13 -15 . . 1.00 72.99 B C

. - -14.4361.00 73.05 B O
ATOM 2948N ARGB .

116-2.812 -14.554-15.5081.00 73.04 B N

ATOM 2949CA ARGB 116-2.530 -15.619-14 1 72 B

. . . C
ATOM 2950CB ARGB 116-3.632 -16 -14 . . 1.00 72.91 B C
ATOM 2g51CG ARGB 116-4 -16 . . -13.6591.00 73.17 B C

-4.gg2 -15.738-12.1941.00 72.86 B C
ATO

M 2953NE ARGB 116-6.284 -15.223-11.7681 73 8 N

ATOM 2954CZ ARGB 116-6.520 -14.749-10 . .

. , 73.16 B C

. . - 1.00 73.30 B N
ATOM 2956NH2ARGB 116 .

-7.721 -14.285-10.2391.00 73.10 B N
ATOM

2957C ARGB 116-1.194 -16.347-14.4231 72 B

. . C

. . -13.9741.00 72.92 B O

ATOM 2959N PROB 117-0.179 -15.699-15.0211.00 71.60 B N
ATOM 2960~ PROB 117-0.071 -14.272-15.3721.00 71.34 B C
ATOM 2961CD PROB 1171.120 -16.361-15.1691.00 70.77 B C
ATOM 2962CA PROB 1171.984 -15.276-15.8031.00 71.04 B C
ATOM 2963CB PROB 1171.408 -14.024-15.2341.00 70.92 B C
ATOM 2964CG PROB 1171.701 -16.874-13.8541.00 70.28 B C
ATOM 2965C PROB 1172.333 -17.930-13.8131.00 70.37 B O
ATOM 2966O LEUB 1181.476 -16.125-12.7821.00 69.38 B N
ATOM 2967N LEUB 1181.987 -16.506-11.4741.00 68.52 B C
ATOM 2968CA LEUB 1181.873 -15.331-10.4981.00 67.49 B C
ATOM 2969CB LEUB 1182.359 -15.607-9.0731.00 66.88 B C
ATOM 2970CG LEUB 1183.814 -16.038-9.1041.00 66.80 B C
ATOM 2971CD1LEUB 1182.183 -14.366-8.2211.00 66.85 B C
ATOM 2972CD2LEUB 1181.251 -17.715-10.9071.00 68.13 B C
ATOM 2973C LEU8 1181.871 -18.627-10.3641.0D 67.55 B O
ATOM 29740 THRB 119-0.070 -17.720-11.0381.00 68.22 B N
ATOM 2975N THRB 119-0.884 -18.809-10.5211.00 68.37 B C
ATOM 2976CA THRB 119-2.388 -18.469-10.6091.00 68.91 B C
ATOM 2977CB THRB 119-2.678 -17.367-9.7391.D0 70.12 B O
ATOM 2978OG1THRB 119-3.235 -19.659-10.1881.00 69.22 B C
ATOM 2979CG2THRB 119-0.641 -20.144-11.2151.00 68.02 B C
ATOM 2980C THRB 119-0.566 -21.179-10.5571.00 68.04 B O
ATOM 2981O VALB 120-0.596 -20.128-12.5371.00 67.78 B N
ATOM 2982N VALB 120-0.294 -21:367-13:2771.00 68.05 B C
ATOM 2983CA VALB 120-0.601 -21.190-14.7771.00 67.87 B C
ATOM 2984CB VALB 120-2.085 -20.937-14.9671.00 67.50 B C
ATOM 2985CG1VALB 1200.204 -20.038-15.3421.00 68.78 B C
ATOM 2986CG2VALB 1201.122 -21.914-13.1121.00 68.05 B C
ATOM 2987C VALB 1201.294 -23.081-12.7631.00 68.85 B O
ATOM 2988O ILEB 1212.131 -21.085-13.3561.00 67.67 B N
ATOM 2989N ILEB 1213.511 -21.528-13.2041.00 67.18 B C
ATOM 2990CA ILEB 1214.499 -20.365-13.4321.00 65.84 B C
ATOM 2991CB ILEB 1215.925 -20.838-13.1891.00 64.74 B C
ATOM 2992CG2ILEB 1214.355 -19.829-14.8571.00 64.51 B C
ATOM 2993CG1ILEB 1215.303 -18.701-15.1851.00 63.78 B C
ATOM 2994CDtILEB 1213.728 -22.089-11.7991.00 68.01 B C
ATOM 2995C ILEB 1214.500 -23.025-11.6031.00 68.45 B O
ATOM 2996O MET8 1223.032 -21.516-10.8241.00 68.60 B N
ATOM 2997N METB 1223.152 -21.959-9.4421.00 69.44 B C
ATOM 2998CA METB 1222.556 -20.913-8,4921.00 68.29 B C
ATOM 2999CB METB 1223.459 -19.725-8.2091.00 66.60 B C
ATOM 3000CG METB 1224.905 -20.181-1.2461.00 65.71 B S
ATOM 3001SD METB 1224.264 -20.072-5.5761.00 63.38 B C
ATOM 3002CE METB 1222.452 -23.294-9.2271.00 70.77 B C
ATOM 3003C METB 1222.955 -24.163-8.5101.00 70.43 B O
ATOM 3004O HISB 1231.286 -23.455-9.8431.00 72.35 B N
ATOM 3005N HISB 1230.524 -24.692-9.7011.00 73.74 B C
ATOM 3006CA HISB 123-0.855 -24.554-10.3451.00 74.73 B C
ATOM 3007CB HISB 123-1.640 -25.827-10.3461.00 75.69 B C
ATOM 3008CG HISB 123-2.144 -26.563-11.3651.00 75.96 B C
ATOM 3009CD2HISB 123-1.964 -26.501-9.1881.00 76.18 B N
ATOM 3010ND1HISB 123-2.632 -27.599-9.4931.00 76.66 B C
ATOM 3011CE1HISB 123-2.755 -27.661-10.8071.00 76.84 B N
ATOM 3012NE2HiSB 1231.255 -25.869-10.3281.00 73.69 B C
ATOM 3013C HISB 1231.240 -26.977-9.7941.00 73.99 B O
ATOM 3014O THRB 1241.887 -25.621-11.4681.00 73.42 B N
ATOM 3015N THRB 1242.631 -26.656-12.1681.00 73.24 B C
ATOM 3016CA THRB 1243.096 -26.165-13.5491.00 72.93 B C
ATOM 3017CB THRB 1241.995 -25.564-14.2411.00 72.35 B O
ATOM 3018OG1THRB 1243.630 -27.327-14.3671,00 72.51 B C
ATOM 3019CG2THRB 1243.863 -27.032-11.3541.00 73.28 B C
ATOM 3020C THRB 1244.012 -28.172-10.9171.00 73.29 8 O
ATOM 3021O ILEB 1254.738 -26.054-11.1571.00 73.05 B N
ATOM 3022N ILEB 1255.969 -26.251-10.4091.00 73.14 B C
ATOM 3023CA ILEB 1256.664 -24.895-10.1321.00 72.57 B C
ATOM 3024CB ILE8 1257.821 -25.077-9.1411.00 71.72 B C
ATOM 3025CG2ILEB 1257.149 -24.292-11.4531.00 71.58 B C
ATOM 3026CG1ILEB 1257.837 -22.955-11.3011.00 71.38 B C
ATOM 3027CD1ILEB 1255.737 -26.972-9.0911.00 73.81 B C
ATOM 3028C ILEB 1256.533 -27.819-8.6911.00 74.06 B O
ATOM 3029O PHEB 1264.646 -26.639-8.4141.00 74.73 B N
ATOM 3030N PHEB 1264.349 -27.271-7.1351.00 75.88 B C
ATOM 3031CA PHEB 1263.217 -26.526-6.4151.00 74.21 B C
ATOM 3032CB PHEB 1263.707 -25.458-5.4781.00 72.62 B C
ATOM 3033CG PHEB 1264.404 -24.356-5.9611.00 71.49 B C
ATOM 3034CD1PHEB 1263.521 -25.584-4.1061.00 71.70 B C
ATOM 3035CD2PHEB 1264.909 -23.401-5.0941.00 70.96 B C
ATOM 3036CE1PHEB 1264.024 -24.630-3.2301.00 71.02 B C
ATOM 3037CE2PHEB 1264.721 -23.538-3.7261'.00 70.84 B C
ATOM 3038CZ PHEB 1264.012 -28.749-7.2751.00 77.31 B C
ATOM 3039C PHEB 1264.472 -29.571-6.4771.00 77.75 B O
ATOM 3040O GLNB 1273.215 -29.093-8.2831.00 78.44 B N
ATOM 3041N GLNB 1272.866 -30.490-8.4951.00 79.90 B C
ATOM 3042CA GLNB 1271.795 X0.627-9.5811.00 80.34 B C
ATOM 3043CB GLNB 1270.410 -30.198-9.1211.00 81.93 B C
ATOM 3044CG GLNB 127-0.705 -30.952-9.8261.00 82.60 B C
CD

ATOM 3045OE1GLNB 127-0.89230.828 -11.0391.00 82.86 B 0 ATOM 3046NE2GLNB 127-1.45031.747 __ 1.00 82.24 B N
-9.064 ATOM 3047C GLNB 1274.110 -31.288-8.8791.00 80.52 B C

ATOM 3048O GLNB 1274.324 -32.395-8.3791.00 80.83 B O

ATOM 3049N GLUB 1284.93_3-30.717-9.7551.00 80.48 B N

ATOM 3050CA GLUB 1286.155 -31.377-10.1 1.00 80.52 B C

ATOM 3051CB GLUB 1286.946 -30.462_ 1.00 80.86 B C
-11.133 ATOM 3052CG GLUB 1285.266 -31.062-11.5971.00 81.66 B C

ATOM 3053CD GLU' 1288.927 -30.260-12.7021.00 51.67 B C
B

ATOM 3054OE1GLU. 1289.142 -29.046-12.5151.00 51.36 B O
B

ATOM 3055OE2GLUB 1289.236 -30.851-13.7581.00 82.05 B O

ATOM 3056C GLUB 1287.033 -31.799-9.0151.0D 80.36 B C

ATOM 3057O GLUB 1287.340 -32.981-8.8581.00 80.73 B O

ATOM 3058N ARGB 1297.439 -30.840-8.1881.00 80.10 B N

ATOM 3059CA ARGB 1298.279 -31.146-7.0321.00 80.15 B C

ATOM 3060CB ARGB 1298.902 -29.861-6.4761.00 79.46 B C

ATOM 3061CG ARGB 1299.931 -29.232-7.4081.00 78.39 B C

ATOM 3062CD ARGB 12910.391-27.872-6.9041.00 77.39 B C

ATOM 3063NE ARGB 12911.378-27.259-7.7921.00 76.32 B N

ATOM 3064CZ ARGB 12912.664-27.593-7.8381.00 75.74 B C

ATOM 3065NH1ARGB 12913.143-28.542-7.0411.00 75.99 B N

ATOM 3066NH2ARGB 12913.477-26.974-8.6811.00 74.52 B N

ATOM 3067C ARGB 1297.476 31.866 -5.9451.00 80.55 B C

ATOM 3068O ARGB 1297.943 -32,046-4.8181.00 79.96 B O

ATOM 3069N ASPB 1306.264 -32.277-6.3151.00 81.46 B N

ATOM 3070CA ASPB ' 5.369 -32.998-5.4151.00 82.13 B C

ATOM 3071CB ASPB 1305.867 -04.438-5.2451.00 82.48 B C

ATOM 3072CG ASPB 1304.840 -35.340-4.5901.00 82.66 B C

ATOM 3073OD1ASPB 1303.737 -35.503-5.1571.00 82.91 B O

ATOM 3074OD2ASPB 1305.140 -35.890-3.5101.00 82.59 B 0 ATOM 3075C ASPB 1305.296 -02.303-4.0601.00 82.34 B C

ATOM 3076O ASPB 1305.278 -32.954-3.0141.00 82.47 B O

ATOM 3077N LEUB 1315251 -30.975-4,0951.00 82.38 B N

ATOM 3078CA LEUB 1315.192 -30.166-2.8851.00 82.38 B C

ATOM 3079CB LEUB 1315.565 -28.720-3.2091.00 82.71 B C

ATOM 3080CG LEUB 1316.989 -28.542-3.7421.00 83.08 B C

ATOM 3081CD1LEUB 1317.203 -27.103-4.1861.00 83.45 B C

ATOM 3082CD2LEUB 1317.987 -28.932-2.6571.00 82.80 B C

ATOM 3053C LEUB 1313.824 -30.211-2.2231.00 82.36 B C

ATOM 3084O LEUB 1313.705 -29.964-1.0231.00 82.04 B O

ATOM 3085N LEUB 1322.791 -30.520-3.0041.00 82.60 B N

ATOM 3086CA LEUB 1321.441 -30.606-2.4591.00 82.96 B C

ATOM 3087CB LEUB 1320.396 -30.725-3.5721.00 82.86 B C

ATOM 3088CG LEUB 1320.134 -29.489--0.4311.00 82.50 B C

ATOM 3089CD1LEUB 1321.324 -29.249-5.3351.00 83.01 B C

ATOM 3090CD2LEUB 132-1.125-29.690-5.2591.00 82.72 B C

ATOM 3091C LEUB 1321.346 -31.817-1.5471.00 83.29 B C

ATOM 3092O LEUB 1320.792 -01.733-0.4521.00 83.59 B O

ATOM 3093N LYSB 1331.892 -32.943-2.0001.00 83,77 B N

ATOM 3094CA LYSB 1331.873 -34.169-1.2061.00 83.78 B C

ATOM 3095CB LYSB 1332.054 -35.395-2.1081.00 84.23 B C

ATOM 3096CG LYSB 1330.921 -35.592-3.1001.00 55.29 B C

ATOM 3097CD LYSB 1331.143 -36.798-3.9971.00 85.74 B C

ATOM 3098CE LYSB 1330.017 -36.915-5.0141.00 86.15 B C

ATOM 3099NZ LYSB 1330.238 -38.011-5.9961.00 86.73 B N

ATOM 3100C LYSB 1332.959 -34.146-0.1361.00 83.32 B C

ATOM 3101O LYSB 1332.777 -34.6940.951 1.00 83.45 B O

ATOM 3102N THRB 1344.083 -33.502-0.4391.00 82.98 B N

ATOM 3103CA THRB 1345.192 33.415 0.508 1.00 82.96 B C

ATOM 3104CB THRB 1346.414 32.706 -0.1261.00 83.09 B C

ATOM 3105OG1THRB 1346.913 -33.492-1.2171.00 83.31 B O

ATOM 3106CG2THRB 1347.520 -32.5180.905 1.00 82.68 B C

ATOM 3107C THRB 1344.812 -32.6861.802 1.00 83.02 B C

ATOM 3108O THRB 1345.137 -33.1432.899 1.00 82.72 B p ATOM 3109N PHEB 1354.122 -31.5561.673 1.00 83.12 B N

ATOM 3110CA PHEB 1353.716 -30.7732.838 1.00 83.10 B C

ATOM 3111CB PHEB 1354.178 -29.3232.673 1.00 82.58 B C

ATOM 3112CG PHEB 1355.668 -29.1712.647 1.00 82.20 B C

ATOM 3113CD1PHEB 1356.410 -29.2803.819 1.00 52.05 B C

ATOM 3114CD2PHEB 1356.338 -28.9711.445 1.00 81.76 B C

ATOM 3115CE1PHEB 1357.798 -29.1953.794 1.00 82.11 B 'C

ATOM 3116CE2PHEB 1357.727 -28.8861.409 1.00 81.68 B C

ATOM 3117CZ PHEB 1358.459 -28.9992.585 1.00 81.75 B C

ATOM 3118C PHEB 1352.210 30.815 3.056 1.0D 83.41 B C

ATOM 3119O PHEB 1351.675 -30.0933.898 1.00 83.19 B 0 ATOM 3120N LYSB 1361.535 -31.6712.296 1.00 83.84 B N
ATOM 3121CA LYSB 1360.089 -01.8132.395 1.00 84.32 B C

ATOM 3122CB LYSB 136-0.305-32.3373.784 1.00 84.91 B C
ATOM 3123CG LYS8 1360.417 -33.6114.230 1.00 85.54 B C
ATOM 3124CD LYSB 1360.087 -34.8183.356 1.00 86.42 B C
ATOM 3125CE LYSB 1360.840 -36.0583.835 1.00 86.80 B C
ATOM 3126NZ LYSB 1360.617 -37.2532.968 1.00 86.52 B N
ATOM 3127C LYSB 136-0.577-30.4612.144 1.00 84.16 B C
ATOM 3128O LYSB 136-1.253-29.9193.014 1.0D 84.10 B O
ATOM 3129N ILEB 137-0.369-29.9130.952 1.00 84.21 B N
ATOM 3130CA ILEB 137-0.958-28.6300.583 1.00 83,98 B C

ATOM3131CB ILEB 137-0.023 -27.817-0.340 1.00 83.84 B C

ATOM3132CG2ILEB 137-0.750 -26.582-0.860 1.00 83.99 B C

ATOM3133CG1ILEB 1371:241 -27.4110.414 1.00 83.32 B C

ATOM3134CD1ILEB 1372.260 -26.721-0.463 1.00 83.13 B C

ATOM3135C ILEB 137-2.267 -28.860-0.163 1.00 83.91 B C

ATOM3136O ILEB 137-2.265 -29.273-1.326 1.00 83.62 B O

ATOM3137N PROB 138-3.404 -28.5920.496 1.00 83.80 B N

ATOM3138CD PROB 138-3.558 -28.0061.838 1.00 83.54 B C

ATOM3139CA PROB 138-4.708 -28.783-0.148 1.00 83.99 B C

ATOM3140CB PROB 138-5.695 -28.3160.926 1.00 83.58 B C

ATOM3141CG PROB 1_38-4.894 -27.3301.729 1.00 83.81 B C

ATOM3142C PROB 138-4.815 -27.986-1.448 1.00 84.13 B C

ATOM3143O PROB 138-4.699 -26.761-1.443 1.00 84.35 B O

ATOM3144N VALB 139-5.025_-28.694-2.557 1.00 54.50 B N

ATOM3145CA VAL8 139-5.132 -28.066-3.873 1.00 84.50 B C

ATOM3146CB VALB 139-5.768 -29.028-4.905 1.00 84.60 B C

ATOM3147CG1VALB 139-4.920 -30.281-5.034 1.00 84.87 B C

ATOM3148CG2VALB 139-7.182 -29.390-4.485 1.00 84.92 B C

ATOM3149C VALB 139-5.943 -26.776-3.826 1.00 84.29 B C

ATOM31500 VALB 139-5.651 -25.829-4.555 1.00 84.62 B O

ATOM3151N ASPB 140-6.960 -26.744-2.969 1.00 84.16 B N

ATOM3152CA ASPB 140-7.794 -25.558-2.816 1.0D 83.44 B C

ATOM3153CB ASPB 140-8.896 -25.786-1.776 1.0D 83.96 B C

ATOM3154CG ASPB 140-10.003-26.681-2.282 1.00 84.45 B C

ATOM3155OD1ASPB 140-9.759 -27.891-2.461 1.00 85.38 B O

ATOM3156OD2ASPB 140-11.122-26.172-2.504 1.00 85.02 B O

ATOM3157C ASPB 140-6.915 -24.416-2.344 1.00 82.94 B C

ATOM3158O ASPB 140-6.514 -23.560-3.134 1.00 83.62 B O

ATOM3159N THRB 141-6.615 -24.423-1.047 1.00 81.54 B N

ATOM3160CA THRB 141-5.786 -23.397-0.430 1.00 80.24 B C

ATOM3161CB THRB 141-5.132 -23.9210.869 1.00 80.20 B C

ATOM3162OG1THRB 141-6.145 -24.4461.735 1.00 79.79 B O

ATOM3163CG2THRB 141-4.406 -22.7971.593 1.00 79.97 B C

ATOM3164C THRB 141-4.695 -22.888-1.374 1.00 79.12 B C

ATOM3165O THRB 141-4.671 -21.706-1.707 1.00 79.26 B O

ATOM3166N LEUB 142-3.810 -23.776-1.819 1.00 77.82 B N

ATOM3167CA LEUB 142-2.723 -23.380-2.714 1.00 76.47 B C

ATOM3168CB LEUB 142-2.070 -24.606-3.359 1.00 76.04 B C

ATOM3169CG LEUB 142-0.963 -24.259-4.361 1.00 75.28 B C

ATOM3170CD1LEUB 1420.142 -23.496-3.659 1.00 75.07 B C

ATOM3171CD2LEU.B142-0.415 -25.521-4.986 ___ 75,37 B C
1.00 ATOM3172C LEUI 142-3.168 -22.427-3.815 1.00 75.51 B C
B

ATOM3173O LEUi 142-2.604 -21.345-3.979 1.00 7 B O
B 5.26 ATOM3174N ILEi 143-4.175 -22.832-4.576 1.00 _ B N
B 74.D3 ATOM3175CA ILE~ 143-4.673 -22.001-5.658 1.00 73.06 B C
B

ATOM3176CB ILEB 143-5.720 -22.757-6.481 1.00 72.61 B C

ATOM3177CG2ILEB 143-6.409 -21.811-7.448 1.00 72.20 B C

ATOM3178CG1ILEB 143-5.038 -23.910-7.222 1.00 72.49 B C

ATOM3179CD1ILEB 143-5.993 -24.831-7.948 1. 72.80 B C

ATOM3180C ILEB 143-5.275 -20.703-5.138 _ 72.86 B C
1.00 ATOM3181O ILEB 143-5.066 -19.6425.720 1.00 72.80 B O

ATOM' N THRB 144-6.011 -20.791-9.035 1.00 72.47 B N

ATOM3183CA THRB 144-6.647 -19.622-3.440 1.00 72.38 B C

ATOM3184CB THRB 144-7.581 -20.034-2.274 1.00 72,91 B C

ATOM3185OGtTHRB 144-8.680 -20.794-2.793 1.00 72.91 B O

ATOM3186CG2THRB 144-8.126 -18.804-1.552 1.00 73.33 B C

ATOM3187C THRB 144-5.637 -18.576-2.950 1.00 71.84 B C

ATOM3188O THRB 144-5.913 -17.376-2.993 1.00 72.17 B O

ATOM3189N TYRB 145-4.474 -19.022-2.482 1.00 70.72 B N

ATOM3190CA TYRB 145-3.452 -18.089-2.021 1.00 69.34'B C

ATOM3191CB TYRB 145-2.378 -18.797-1.213 1.00 67,89 B C

ATOM3192CG TYRB 145-1.201 -17.898-0.921 1.00 66.88 B C

ATOM3193CD1TYRB 145-1.199 -17.0660.193 1.00 66.17 B C

ATOM3194CE1TYRB 145-0.132 -16.2130.451 1.00 65.66 B C

ATOM3195CD2TYRB 145-0.102 -17.853-1.779 1.00 66.15 B C

ATOM3196CE2TYRB 1450.971 -17.001-1.530 1.00 65.36 B C

ATOM3197CZ TYRB 1450.947 -16.186-0.412 1.00 65.14 B C

ATOM3198OH TYRB 1452.002 -15.353-0.141 1.00 64.73 B O

ATOM3199C TYRB 145-2.784 -17.454-3.230 1.00 69.37 B C

ATOM3200O TYRB 145-2.557 -16.245-3.272 1.00 69.61 B 0 ATOM3201N LEUB 146-2.450 -18.295-4.202 1.00 69.06 B N

ATOM3202CA LEUB 146-1.805 -17.848-5.425 1.00 68.27 B C

ATOM3203CB LEUB 146-1.613 -19.032-6.379 1.00 67.70 B C

ATOM3204CG LEUB 146-0.757 -20.194-5.864 1.00 67.78 B C

ATOM3205CD1LEUB 146-0.812 -21.351-6.852 1.00 67.12 B C

ATOM3206CD2LEUB 1460.677 -19.726-5.651 1.D0 67.20 B C

ATOM3207C LEUB 146-2.653 -16.779-6.095 1.00 67.93 B C

ATOM32080 LEUB 146-2.127 -15.836-6.681 1.00 67.88 B 0 ATOM3209N METB 147-3.969 -16.924-6.002 1.00 67.69 B N

ATOM3210CA METB 147-4.869 -15.960-6.619 1.00 67.67 B C

ATOM3211CB METB 147-6.252 -16.580-6.814 1.00 68.06 B C

ATOM3212CG METB 147-6.249 -17.804-7.722 1.00 68.19 B C

ATOM3213SD METB 147-7.902 -18.454-8.061 1.00 68.45 B S

ATOM3214CE METB 147-7.960 -18.296-9.867 1.00 68.01 B C

ATOM3215C METB 147-4.966 -14.685-5.786 1.00 67.30 B C

ATOM3216O METB 147-5.082 -13.587-6.327 1.00 67.05 B O

ATOM 3217N THRB 148-4.916 -14.826-4.468 1.00 66.97 B N

ATOM 3218CA THRB 148-4.976 -13.655-3.605 1.00 66.85 B C

ATOM 3219CB THRB 148-5.110 -14_.054-2,119 1.00 67.08 B C

ATOM 3220OG1THRB 148-6.212 -14.957-1.965 1.00 68.25 B O

ATOM 3221CG2THRB 148-5.361 -12.820-1.255 1.00 66.71 B C

ATOM 3222C THRB 148-3.675 -12.875-3.811 1.00 66.15 B C

ATOM 32230 THRB 148-3.686 -11.656-3.968 1.00 66.20 B O

ATOM 3224N LEUB 149-2.558 -13.599-3.825 1.00 65.20 B N

ATOM 3225CA LEUB 149-1.244 -13.000-4.023 1.00 63.91 B C

ATOM 3226CB LEUB 149-0.158 -14.075-3.903 1.00 63.31 B C

ATOM 3227CG LEUB 1491.291 -13.631-4 1.00 63.23 B C

ATOM 3228CD1LEUB 1491.657 -12.564_ 1.00 62.28 B C
-3.122 ATOM 3229CD2LEUB 1492.237 -14.828-4.013 1.0D 62.35 B C

ATOM 3230C LEUB 149-1.136 -12.310-5.386 1.00 62.96 B C

ATOM 3231O LEUB 149-0.705 -11.162-5.477 1.00 62.65 B 0 ATOM 3232N GLUB 150-1.536 -13.006-6.442 1.00 61.89 B N

ATOM 3233CA GLUB 150-1.459 -12.440-7.778 1.00 61.74 B C

ATOM 3234CB GLUB 150-1.912 -13.465-8.818 1.00 62.06 B C

ATOM 3235CG GLUB 150-1.818 -12.950-10.2451.00 63.32 B C

ATOM 3236CD GLUB 150-1:632 -14.062-11.2571.00 64.55 B C

ATOM 3237OE1GLUB 150-2.467 -14.989-11.2751.00 65.58 B O

ATOM 3238OE2GLUB 150-0.652 -14.009-12.0331.00 63.96 B O

ATOM 3239C GLUB 150-2.280 -11.164-7,916 1.00 61.24 B C

ATOM 3240O GLUB 150-1.816 -10.174-8.488 1.00 60.34 B O

ATOM 3241N ASPB 151-3.506 -11.195-7.402 1.00 60.67 B N

ATOM 3242CA ASPB 151-4,386 -10.034-7.459 1.00 59.12 B C

ATOM 3243CB ASPB 151-5.735 -10.357-6.818 1.00 60.76 B C

ATOM 3244CG ASPB 151-6.552 -11.322-7.642 1.00 61.97 B C

ATOM 3245OD1ASPB 151-7.545 -11.869-7.112 1.00 63.08 B O

ATOM 3246OD2ASPB 151-6.203 -_11.527-8.821 1.00 62.83 B O

ATOM 3247C ASPB 151-3.750 -8.858-6.726 1.00 57.66 B C

ATOM 3248O ASPB 151-4.057 -7.702-7.018 1.00 57.14 B O

ATOM 3249N HISB 152-2.869 -9.154-5.771 1.00 55.28 B N

ATOM 3250CA HISB 152-2.206 -8.099-5.021 1.00 53.15 B C

ATOM 3251CB HIS: 152-1.893 -8.565-3.600 1.00 53.90 B C
B

ATOM 3252CG HISB 152-3.061 -8.456-2.672 1.00 55.38 B C

ATOM 3253CD2HIS~ 152-3.179 -7.896-1.444 1.00 56.24 B C
B

ATOM 3254ND1HISB 152-4.310 -5.949-2.989 1.00 56.21 B N

ATOM 3255CE1HISB 152-5.146 -8.697-1.996 1.00 56.33 B C

ATOM 3256NE2HISB 152-4.485 -8.060-1.047 1.00 56.86 B N

ATOM 3257C HISB 152-0.965 -7.533-5.700 1.00 51.10 B C

ATOM 3258O HISB 152-0.118 -6.920-5.059 1.00 49.57 B O

ATOM 3259N TYRB 153-0.870 -7.757-7.005 1.00 49.78 B N

ATOM 3260CA TYRB 1530.207 -7.205-7.820 1.00 49.85 B C

ATOM 3261CB TYRB 1530.864 -8.277-8.707 1.00 49.22 B C

ATOM 3262CG TYRB 1532.069 -8.946-8.074 1.00 48.55 B C

ATOM 3263CD1TYRB 1531.916 -9.964-7,129 1.0D 49.05 B C

ATOM 3264CE1TYRB 1533.023 -10.548~ -6.5051.00 47.84 B C

ATOM 3265CD2TYRB 1533.364 -8.531-8.384 1.00 47.99 B C

ATOM 3266CE2TYRB 1534.476 -9.108-7.765 1.00 46.84 B C

ATOM 3267CZ TYRB 1534.296 -10.110-6.827 1.00 47.20 B C

ATOM 3268OH TYRB 1535.384 -10.658-6.183 1.00 48.34 B O

ATOM 3269C TYRB 153-0.535 -6.183-8.681 1.00 49.59 B C

ATOM 3270O TYRB 153-1.585 -6.494-9.246 1.00 50.05 B 0 ATOM 3271N HISB 154-0.013 -4.967-8.775 1.00 49.14 B N

ATOM 3272CA HISB 154-0.694 -3.926-9.544 1.00 48.69 B C

ATOM 3273CB HISB 154-0.119 -2.549-9.188 1.00 48.06 B C

ATOM 3274CG HISB 154-0.094 -2.266-7.717 1.00 47.76 B C

ATOM 3275CD2HISB 154-0.402 -3.045-6.652 1.00 47.70 B C

ATOM 3276ND1HISB 1540.338 -1.066-7.198 1.00 48.02 B N

ATOM 3277CE1HISB 1540.299 -1.119-5.878 1.00 48.49 B C

ATOM 3278NE2HISB 154-0.146 -2.311-5.522 1.00 47.87 B N

ATOM 3279C HISB 154-0.641 -4.132-11.0561.00 49.24 B C

ATOM 3280O HISB 1540.433 -4.169-11.6511.00 49.87 B O

ATOM 3281N ALAB 155-1.815 -4.249-11,6681.00 49.47 B N

ATOM 3282CA ALAB 155-1.937 -4.447-13.1101.00 48.88 B C

ATOM 3283CB ALAB 155-3.374 -4.838-13.4561.00 48.44 B C

ATOM 3284C ALAB 155-1.531 -3.206-13.9081.00 47.86 B C

ATOM 3285O ALAB 155-1.265 -3.289-15.1111.00 46.79 B O

ATOM 3286N ASPB 156-1.490 -2.059-13.2331.00 46.87 B N

ATOM 3287CA ASPB 156-1.124 -0.797-13.8761.00 46.24 B C

ATOM 3288CB ASPB 156-1.718 0.389 -13,0931.00 46.48 B C

ATOM 3289CG ASPB 156-1.568 0.234 -11.5871.00 46.49 B C

ATOM 3290OD1ASPB 156-2.040 -0.790-11.0551.00 46.27 B O

ATOM 3291OD2ASPB 156-0.987 1.132 -10.9311.00 48.17 B O

ATOM 3292C ASPB 1560.387 -0.624-14.0121.00 45.13 B C

ATOM 3293O ASPB 1560.866 0.113 -14.8741.00 46.35 B O

ATOM 3294N VALB 1571.136 -1.308-13.1611.00 43.40 B N

ATOM 3295CA VALB 1572.584 -1.218-13.1901,00 42.17 B C

ATOM 3296CB VALB 1573.165 -1.695-11.8401.00 42.10 B C

ATOM 3297CG1VALB 1574.678 -1.717-11.8881.00 41.45 B C

ATOM 3298CG2VALB 1572.682 -0.765-10.7251.00 37.80 B C

ATOM 3299C VALB 1573.089 -2.064-14.3541.00 42.06 B C

ATOM 33000 VALB 1572.735 -3.243-14.4771.00 42.49 B 0 ATOM 3301N ALAB 1583.907 -1.460-15.2131.00 40.73 B N

ATOM 3302CA ALAB 1584.413 -2.157-16.3951.00 39.83 B C

ATOM 3303CB ALAB 1584.998 -1.149-17.3851.00 39.69B C

ATOM 3304C ALAB 1585.428 -3.25716.112 1.00 39.21B C

ATOM 33050 ALAB 1585.427 -4.287-16.7911.00 38.06B O

ATOM 3306N TYRB 1596.283 -3.047-15.1131.0D 38.82B N

ATOM 3307CA TYRB 1597.304 -4.038-14.7691.00 39.09B C

ATOM 3308CB TYRB 1598.652 -3.357-14.5401.00 38.04B C

ATOM 3309CG TYRB 1599.776 -4.346-14.3761.00 38.65B C

ATOM 3310CD1TYRB 15910.32fi-4,996-15.4841.00 38.72B C

ATOM 3311CE1TYRB 15911.346 -5.931-15.3341.00 37.89B C

ATOM 3312CD2TYRB 15910.274 -4.660-13.1151,00 38.64B C

ATOM 3313CE2TYRB 15911.290 -5.595-12:9541.00 37.72B C

ATOM 3314CZ TYRB 15911.823 -6.224-14.0651.00 38.61B C

ATOM 3315OH TYRB 15912.845 -7.135-13.9031.00 37.58B O

ATOM 3316C TYRB 1596.990 -4.906-13.5471.00 39.69B C

ATOM 3317O TYRB 1596.621 -6.077-13.6831.00 40.24B O

ATOM 3318N HISB 1607.151 -4.317-12.3631.00 39.67B N

ATOM 3319CA HISB 1606.931 -4.989-11.0861.00 40.52B C

ATOM 3320CB HISB 1607.297 -4.038-9.946 1.00 38.72B C

ATOM 3321CG HISB 1608.703 -3.533-10.0141.00 39.268 C

ATOM 3322CD2HISB 1609.870 -4.083-9.598 1.00 39.84B C

ATOM 3323ND1HISB 1609.035 -2.330-10.5961.00 38.99.B N

ATOM 3324CE1HISB 16010.343 -2.157-10.5351.00 38.71B C

ATOM 3325NE2HIS, 16010.875 -3.207-9.934 1.00 39.82B N
B

ATOM 3326C HIS- 1605.527 -5.546-10.8511.00 41.81B C
B

ATOM 3327O HISB 1604.849 -5.172-9.888 1.00 41.22B O

ATOM 3328N ASNB 1615.109 -6_.471-11:7061.00 42.96B N

ATOM 3329CA ASNB 1613.790 -7.063-11.5931.00 44.59B C

ATOM 3330CB ASNB 1612.935 -6.567-12.7491.00 45.63B C

ATOM 3331CG ASNB 1613.589 -6.819-14.0901.00 48.81B C

ATOM 3332OD1ASNB 1613.817 -7.967-14:4671.00 50,42B O

ATOM 3333ND2ASNB 1613.909 -5.745-14.8161.00 49.09B N

ATOM 3334C ASNB 1613.839 -8.596-11.5881.00 45.24B C

ATOM 3335O ASNB 1614.908 -9.195-11.5461.00 45.09B O

ATOM 3336N ASNB 1622.657 -9.203-11.64?.1.00 45.45B N

ATOM 3337CA ASNB 1622.467 -10.652-11.6381.00 45.63B C

ATOM 3338CB ASNB 1620.983 -10.967-11.8561.00 45.63B C

ATOM 3339CG ASNB 1620.492 -10.535-13.2281.00 46.54B C

ATOM 3340OD1ASNB 1620.939 -9.520-13.7671.00 47.48B O

ATOM 3341ND2ASNB 162-0.440 -11.300-13.7971.00 46.27B N

ATOM 3342C ASNB 1623.303 -11.404-12.6741.00 46.15B C

ATOM 3343O ASNB 1623.724 -12.547-12.4391.00 46.01B O

ATOM 3344N ILEB 1633.534 -10.777-13.8221.00 45.36B N

ATOM 3345CA ILEB 1634.329 -11.417-14.8571.00 44.90B C

ATOM 3346CB ILEB 1634.243 -10.653-16.1851.00 44.43B C

ATOM 3347CG2ILEB 1635.010 -11.412-17.2591.00 44.59B C

ATOM 3348CG1ILEB 1632.773 -10.484-16.5951.00 43.94B C

ATOM 3349CD1ILEB 1632.573 -9.639-17.8351.00 43.06B C

ATOM 3350C ILEB 1635.790 -11.492-14.4001.00 45.53B C

ATOM 3351O ILEB 1636.454 -12.513-14.6021.00 46.27B O

ATOM 3352N HISB 1646.279 -10.418-13.7781.00 43.97B N

ATOM 3353CA HISB 1647.652 -10.373-13,2771.00 43.12B C

ATOM 3354CB HISB 1647.976 -8.976-12.7411.00 41.31B C

ATOM 3355CG HISB 1649.245 -8.906-11.9421.00 41.13B C

ATOM 3356CD2HISB 1649.457 -8.655-10.6271.00 40.74B C

ATOM 3357ND1HISB 16410.493 -9.075-12.5021.00 39.54B N

ATOM 3358CE1HISB 16411.418 -8.928-11.5711.00 38.85B C

ATOM 3359C HISB 1647.807 -11.398-12.1591.00 43.24B C

ATOM 3360O HISB 1648.799 -12.120-12.0951,00 41.85B O

ATOM 3361NE2HISB 16410.817 -8.671-10.4231.00 41.38B N

ATOM 3362N ALAB 1656.814 -11.443-11.2721.00 44.46B N

ATOM 3363CA ALAB 1656.820 -12.376-10.1551.00 44.80B C

ATOM 3364CB ALAB 1655.646 -12,089-9.231 1.00 43.70B C

ATOM 3365C ALAB 1656.7_40 -13.804-10.7061.00 46.31B C

ATOM 3366O ALAB 1657.411 -14.708-10.2121.00 46.57B O

ATOM 3367N ALAB 1665.914 -14.000-11.7321.00 47.66B N

ATOM 3368CA ALAB 1665.784 -15.307-12.3601.00 48.89B C

ATOM 3369CB ALAB 1664.666 -15.288-13.4051.00 49.38B C

ATOM 3370C ALAB 1667.120 -15.650-13.0261.00 49.67B C

ATOM 3371O ALAB 1667.546 -16.810-13.0261.00 50.37B O

ATOM 3372N ASPB 1677.776 -14.630-13.5761.00 49.64B N

ATOM 3373CA ASPB 1679.064 -14.798-14.2441.00 50.33B C

ATOM 3374CB ASPB 1679.4_94 -13.490-14.9231.00 50.17B C

ATOM 3375CG ASPB 16710.757 -13.646-15.7601.00 50.08B C

ATOM 3376OD1ASPB 16710.811 -14.582-16.5801.00 51.80B O

ATOM 3377OD2ASPB 16711.694 -12.833-15.6151.00 49.96B O

ATOM 3378C ASPB 16710.134 -15.225-13.2571.00 51.36B C

ATOM 3379O ASPB 16710.863 -16.176-13.5101.00 51.17B 0 ATOM 3380N VALB 16810.217 -14.528-12.1271.00 52,61B N

ATOM 3381CA VALB 16811.223 -14.829-11.1111.00 53.29B C

ATOM 3382CB VALB 16811.226 -13.751-10.0031.00 51.76B C

ATOM 3383CG1VALB 16812.274 -14.076-8.954 1.00 50.68B C

ATOM 3384CG2VALB 16811.511 -12.396-10.6181.00 51.54B C
ATOM 3385C VALB 16811.046 -16.210-10.4821.00 54.58B C

ATOM 33860 VALB 16812.025 -16.914-10.2351.00 54.058 O

ATOM 3387N VALB 1699.798 -16.594-10.2261.00 56.09B N

ATOM 3388CA VALB 1699.512 -17.896-9.633 1.00 57.18B C

ATOM 3389CB VAL B 1697.993 -18.095~ -9.3851.00 57.77 B C

ATOM 3390CG1VAL B 1697.736 -19.481-8.834 1.00 57.75 B C

ATOM 3391CG2VAL B 1697.477 -17.059-8.411 1.00 58.41 B C

ATOM 3392C VAL B 1699.993 -19.005-10.5671.00 57.48 B C

ATOM 3393O VAL B 16910.658 -19.947-10.1401.00 56.86 B O

ATOM 3394N GLN B 1709.658 -18.880-11.8451.00 57.77 B N

ATOM 3395CA GLN B 17010.045 -19.879-12.8271.00 58.80 B C

ATOM 3396CB GLN B 1709.242 -19.675-14.1151.00 59.25 B C

ATOM 3397CG GLN B 1709.350 -20.812-15.1231.00 60.81 B C

ATOM 3398CD GLN B 17010.515 -20.653-16.0831.00 61.56 B C

ATOM 3399OE1GLN B 17010.646 -19.629-16.7541,00 61.81 B O

ATOM 3400NE2GLN B 17011.360 -21.673-16.1641.00 62.88 B N

ATOM 3401C GLN B 17011.548 -19.846-13.1181.00 59.25 B C

ATOM 3402O GLN B 17012.139 -20.877-13.4401.00 58.91 B 0 ATOM 3403N SER B 17112.164 -18.669-13.0061.00 58.51 B N

ATOM 3404CA SER B 17113.597 -18.547-13.2491.00 58.15 B C

ATOM 3405CB SER B 17114.024 -17.075-13.3401.00 58.19 B C

ATOM 3406OG SER B 17113.613 -16.475-14.5611.00 57.26 B O

ATOM 3407C SER B 17114.311 -19.210-12.0881.00 58.20 B C

ATOM 3408O SER B 17115.327 -19.880-12.2681.00 57.07 B O

ATOM 3409N THR B 17213.763 -19.010-10.8931.00 58.37 B N

ATOM 3410CA THR B 17214.315 -19.590-9.676 1.00 59.25 B C

ATOM 3411CB THR B 17213.554 -19.083-8.433 1.00 59.63 B C

ATOM 3412OG1THR B 17213.676 -17.657-8.346 1.00 60.92 B O

ATOM 3413CG2THR B 17214.115 -19.716-7.165 1.00 60.12 B C

ATOM 3414C THR B 17214.178 -21.107-9.746 1.00 59.40 B C

ATOM 3415O THR B 17215.093 -21.849-9.389 1.00 58.10 B O

ATOM 3416N HIS B 17313.019 -21.553-10.2181.00 60.33 B N

ATOM 3417CA HIS B 17312.726 -22.972-10.3501.00 61.42 B C

ATOM 3418CB HIS B 17311.397 -23.164-11.0721.00 62.13 B C

ATOM 3419CG HIS B 17311.052 -24.597-11.3131.00 62.77 B C

ATOM 3420CD2HIS B 17311.063 -25.338-12.4451.00 62.65 B C

ATOM 3421NDtHIS B 17310.679 -25.452-10.2971.00 63.15 B N

ATOM 3422CE1HIS B 17310.476 -26.658-10.7951.00 63.10 B C

ATOM 3423NE2HIS B 17310.702 -26.616-12.0961.00 63.78 B N

ATOM 3424C HIS B 17313.829 -23.673-11.1301.00 61.81 B C

ATOM 3425O HIS B 17314.441 -24.632-10.6511.00 61.42 B 0 ATOM 3426N VAL B 17414.065 -23.185-12.3431.00 62.04 B N

ATOM 3427CA VAL B 17415.098 -23.727-13.2131.00 62.13 B C

ATOM 3428CB VAL B 17415.208 -22.895-14.5161.00 61.74 B C

ATOM 3429CG1VAL B 17416.261 -23.482-15.4331.00 60.96 B C

ATOM 3430CG2VAL B 17413.865 -22.863-15.2201.00 61.42 B C

ATOM 3431C VAL B 17416.450 -23.722-12.4911.00 62.22 B C

ATOM 3432O VAL B 17417.212 -24.687-12.5811.00 62,73 B O

ATOM 3433N LEU B 17516.739 -22.641-11.7691,00 61.85 B N

ATOM 3434CA LEU B 17518.000 -22.528-11.0441.00 61.87 B C

ATOM 3435CB LEU B 17518.154 -21.126-10.4491.00 61.23 B C

ATOM 3436CG LEU B 17518.351 -19.988-11.4491.00 61.35 B C

ATOM 3437CD1LEU B 17518.630 -18.697-10.6901.00 60.37 B C

ATOM 3438CD2LEU B 17519.503 -20.318-12.3921.00 60.08 B C

ATOM 3439C LEU B 17518.161 -23.569-9.940 1.00 62.04 B C

ATOM 3440O LEU B 17519.278 -24.006-9.658 1.00 62.04 B O

ATOM 3441N LEU B 17617.055 -23.959-9.308 1.00 62.10 B N

ATOM 3442CA LEU B 17617.104 -24.962-8.247 1.00 62 B C

ATOM 3443CB LEU B 17615.795 -24.980-7.456 1.00 . B C
62.00 ATOM 3444CG LEU B 17615.611 -23.940-6.348 1.00 61 B C

ATOM 3445CD1LEU B 17614.188 -24.002-5.832 1.00 . B C
62,00 ATOM 3446CD2LEU B 17616.597 -24.203-5.220 1.00 61 B C
~ 66 ATOM 3447C LEU B 17617.373 -26.350-8.826 1.00 . B C
62.48 ATOM 3448O LEU B 17618.000 -27.190-8.176 1.00 61 B O

ATOM 3449N SER B 17716.891 -26.581-10.0461.00 . B N
63.09 ATOM 3450CA SER B 17717.085 -27.855-10.7361.00 63 B C

ATOM 3451CB SER B 17716.013 -28.061-11 1 . B

. . . C
ATOM 3452OG SER B 17714.744 -28.307-11.2361 64 B O

ATOM 3453C SER B 17718.452 -27.924-11.405. . B C
1.00 64 ATOM 3454O SER B 17715.716 -28.842-12.1801.00 . B O

ATOM 3455N THR B 17819.312 -26.950-11.1141.00 . B N

ATOM 3456CA THR B 17820.648 -26.914-11.6991.00 . B C

ATOM 3457CB THR B 17821.356 -25.564-11.3941.00 . B C

ATOM 3458OG1THR B 17822.613 -25.510-12 1 . B

. . . 0 ATOM 3459CG2THR B 17821.598 -25 -9 . . 1.00 66.75 B C

. . . 1.00 65.76 B C

. . -9.952 1.00 65.79 B O

, -28.880-12.0671.00 66.47 B N

ATOM 3463CD PRO B 17921.862 -28.790-13 1 66 B

. . . C
ATOM 3464CA PRO B 17922.916 -30 -11 . . 1.00 66.80 B C
ATOM 3465CB PRO B 17923.495 -30 -13 . . 1.00 66.14 B C
ATOM 3466CG PRO B 17922.354 -30 -14 . . 1.00 66.07 B C

. . - 1.00 67.55 B C
ATOM 3468O PRO B 17924 -30 .

. . -9.671 1.00 67.81 B O

.910 -28.896-10.8941.00 68.34 B N

ATOM 3470CA ALA B 18025.981 -28.648-9.927 1 68 B C

ATOM 3471CB ALA B 18026.781 -27.412-10 . . B

. . . C
ATOM 3472C ALA B 18025.441 -28.482-8 1 . . 69.45 B C
ATOM 3473O ALA 8 18026.191 -28 -7 . . 1.00 70.62 B O

. - -5.394 1.00 70.10 B N
.

ATOM 3475CA LEUB 181_ 23.496-28.044-7.092 1.00 70.96 B C
_ ATOM 3476CB LEUB 18122.725 -26.717-7.061 1.00 71.18 B C

ATOM 3477CG _LEUB 18123.479 -25.425-6.734 1.00 71.05 B C

ATOM 3478CD1LEUB 18122.589 -24.226-7.039 1.00 71.20 B C

ATOM 3479CD2LEUB 18123_893 -25.431-5.266 1.00 70.40 B C

ATOM 3480C LEUB 18122.532 -29.186-6.778 1.00 70.91 B C

ATOM 3481O LEUB 18121.827 -29.163-5.768 1.0D 70.77 B O

ATOM 3482N GLUB 18222.508 -30.183-7.650 1.00 71.01 B N

ATOM 3483CA GLUB 18221.625 -31.327-7.484 1.00 71.49 B C

ATOM 3484CB GLUB 18221.985 -32.402-8.518 1.00 72.26 B C

ATOM 3485CG GLUB 18220.797 -33.142-9.120 1.00 73.33 B C

ATOM 3486CD GLUi 18221.088 -33.667-10.5241.00 74.89 B C
B

ATOM 3487OE1GLU' 18222.048 -3_4.453-10.6921.00 75.45 B O
B

ATOM 3488OE2GLU; 18220.354 -33.287-11.4621.00 75.41 B O
B

ATOM 3489C GLUI _18_221.698 X1.901-6.069 1.00 70.91 B C
B

ATOM 3490O GLU~ 18222:782 -32.068-5.505 1.00 70.65 B O
B

ATOM 3491N ALA8 18320.527 32.170-5.500 1.00 70.55 B N

ATOM 3492CA ALAI 18320.402 -32.748-4.164 1.00 70.18 B C
B

ATOM 3493CB ALAB 18320.909 -34.200-4.186 1.00 69.77 B C

ATOM 3494C ALAB 18321.073 -31.986-3.016 1.00 69.41 B C

ATOM 3495O ALAB 18321.505 32.600-2.041 1.00 69,61 B O

ATOM 3496N VALB 18421.155 -30.663-3.113 1.00 68.32 B N

ATOM 3497CA VALB 18421.775 -29.876-2.046 1.00 67.01 B C

ATOM 3498CB VALB 18422.537 -28.651-2.602 1.00 66.69 B C

ATOM 3499CG1VALB 18423.067 -27.802-1.449 1.00 65.50 B C

ATOM 3500CG2VALB 18423.679 -29.108-3.495 1.00 66.36 B C

ATOM 3501C VALB 18420.751 -29.368-1.029 1.00 66.42 B C

ATOM 3502O VALB 18420.900 -29.5740.178 1.00 65.76 B O

ATOM 3503N PHEB 185__19.710-28.709-1.530 1.00 65.44 B N

ATOM 3504CA PHEB 18518._6_68_-28.145-0.677 1.00 64.65 B C

ATOM 3505CB PHEB 18518.136 -26.854-1.312 1.00 62.72 B C

ATOM 3506CG PHEB 18519.193 -25.799-1.523 _ 59.66 B C
1.00 ATOM 3507CD1PHEB 18519.793 -25.172-0.441 1.00 58.62 B C

ATOM 3508CD2PHEB 18519.59_1-25.438-2.808 1.00 59.40 B C

ATOM 3509CE1PHEB 18520.773 -24.200-0.630 1.00 57.83 B C

ATOM 3510CE2PHEB 18520.572 -24.464-3.008 1.00 57.94 B C

ATOM 3511CZ PHEB 185_21.162 -23.846-1.916 1.00 57.82 B C

ATOM 3512C PHEB 18517.512 -29.109-0.388 1.00 64.72 B C

ATOM 3513O PHEB 18817.151 -29.942-1.221 1.00 64.65 B O

ATOM 3514N THRB 18616.938 -28.9760.804 1.00 65.20 B N

ATOM 3515CA THRB 18615.834 -29.818_ 1.2521.00 65.70 B C

ATOM 3516CB THRB 18615.789 -29.8882.789 1.00 66.38 B C

ATOM 3517OG1THRB 18615.339______ 3.309 1.00 66.06 B O
-28.630 ATOM 3518CG2THRB 18617.176 -30.1913.353 1.00 66.76 B C

ATOM 3519C THRB 18614.484 -29.2990 1.00 65.89 B C

ATOM 3520O THRB 18614.341 -25.119_ 1.00 66.55 B O
0.458 ATOM 3521N ASPB 18713.494 -30.1870.740 1.00 65.94 B N

ATOM 3522CA ASPB 18712.141 -29.8340.310 1.00 65.68 B C' ATOM 3523CB ASPB 18711.166 -30.9830.599 1.00 66.83 B C

ATOM 3524CG ASPB 18710.927 -31.872-0.607 1.00 68.21 B C

ATOM 3525OD1ASPB 18710.642 -31.335- 1.00 68.66 B O
1.704 ATOM 3526OD2ASPB 18711.004 -33.112_ 1.00 68.65 B O
--0.449 ATOM 3527C ASPB 18711.611 -28.5640.978 1.00 64.67 B C

ATOM 3528O ASPB 18710.813 -27.8350.386 1.00 63.77 B O

ATOM 3529N LEUB 18812.039 -28.309__ 1.00 63.76 B N
2.213 ATOM 3530CA LEUB 18811.589 -_27.1212.933 1.00 63.27 B C

ATOM 3531CB LEUB 18811.840 -27.2614.440 1.00 63.08 B C

ATOM 3532CG LEUB 18811.186 -26.1825.317 1.00 62.53 B C

ATOM 3533CD1LEUB 1889.677 -26.2355.157 1.00 61.64 B C

ATOM 3534CD2LEUB 18811.563 -26.3826.773 1.00 62.46 B C

ATOM 3535C LEUB 18812.300 -25.8772.414 1.00 62.92 B C

ATOM 3536O LEUB 18811.684 -24.8252.247 1.00 63.18 B O

ATOM 3537N GLUB 18913.597 -26.0032.158 1.00 61.97 B N

ATOM 3538CA GLUB 18914.381 -24.8881.654 1.00 60.75 B C

ATOM 3539CB GLUB 18915.862 -25.2551.679 1.00 59.72 B C

ATOM 3540CG GLUB 18916.301 -25.7923.029 1.00 59.52 B C

ATOM 3541CD GLUB 18917.752 -26.2323.063 1.00 58.80 B C

ATOM 3542OE1GLUB 18918.145 -27.0752.228 1.00 57.38 B O

ATOM 3543OE2GLUB 18918.496 -25.7353.937 1.00 58.73 B O

ATOM 3544C GLUB 18913.928 -24.5450.235 1.00 60.63 B C

ATOM 3545O GLUB 18913.905 -23.378-0.150 1.00 60.17 B O

ATOM 3546N ILEB 19013.557 -25.567-0.532 1.00 60.65 B N

ATOM 3547CA ILEB 19013.091 -25.369-1.903 1.00 61.01 B C

ATOM 3548CB ILEB 19012.873 -26.733-2.643 1.00 61.35 B C

ATOM 3549CG2ILEB 19012.031 -26.537-3.902 1.00 60.65 8 C

ATOM 3550CG1ILEB 19014.223 -27.359-3.010 1.00 62.16 B C

ATOM 3551CD1ILEB 19014.107 -28.668-3.801 1.00 61.63 B C

ATOM 3552C ILEB 19011.775 -24.596-1.888 1.00 60.81 B C

ATOM 3553O ILEB 19011.558 -23.713-2.717 1.00 61.23 B O

ATOM 3554N LEUB 19110.900 -24.936-0.944 1.00 60.17 B N

ATOM 3555CA LEUB 1919.609 -24.270-0.823 1,00 59.76 B C

ATOM 3556CB LEUB 1918.763 -24.9290.269 1.00 60.28 B C

ATOM 3557CG LEUB 1917.353 -24.3590.450 1.00 60.40 B C

ATOM 3558CD1LEUB 1916.594 -24.422-0.867 1.00 59.75 B C

ATOM 3559CD2LEUB 1916.627 -25.1421.526 1.00 59.68 B C

ATOM 3560C LEUB 1919.815 -22.799-0.490 1.00 59.05 B C

ATOM 35610 LEU~I~191_ 9.116-21.934_-1.0131.00 58.78B 0 B
~

ATOM 3562N ALA' 19210.775 -22.5200.386 1.00 57.87B N
B

ATOM 3563CA ALAB 19211.081 -21.149_0.760 1.00 57.03B C

ATOM 3564CB ALAB 19212.239 -21.1231.742 1.0D 55.89B C

ATOM 3565C ALAB 19211.434 -20.357-0.501 1.00 56.99B C

ATOM 3566O ALAB 19210.738 -19.408-0.867 1.00 56.92B O

ATOM 3567N ALAB 19312.509 -20.7721.168 1.00 56.60B N

ATOM 3568CA ALAB 19312.981 -20.124-2.387 1.00 55.50B C

ATOM 3569CB ALAB 19313.999 -21.015-3.076 1.00 56.90B C

ATOM 3570C ALAB 19311.846 -19.790-3.352 1.00 55.37B C

ATOM 3571O ALAB 19311.721 -18.652-3.808 1.00 55.94B O

ATOM 3572N ILEB 19411.026 -20.785-3.666 1.00 54.34B N

ATOM 3573CA ILEB 1949.901 -20.596-4.575 1.00 53.78B C

ATOM 3574CB ILEB 1949.246 -21.947-4.927 1:00 53.71B C

ATOM 3575CG2ILEB 1948.016 -21.729- 1.00 52.54B C
5.802 ATOM 3576CG1ILEB 19410.268 -22.832_ 1.00 54.69B C
-5.647 ATOM 3577CD1ILEB 1949.772 -24.238-5.945 1.00 55.62B C

ATOM 3578C ILEB 1948.839 -19.653-3.995 1.00 53.64B C

ATOM 3579O ILEB 1948.300 -18.801-4.705 1.00 54.17B O

ATOM 3580N PHEB 1958.540 -19.801-2.708 1.00 52.33B N

ATOM 3581CA PHEB 1957.550 -18.936-2.071 1.00 52.04B C

ATOM 3582CB PHEB 1957.231 -19.408-0.653 1.00 50.47B C

ATOM 3583CG PHEB 1956.258 -18.5220.065 1.00 49.35B C

ATOM 3584CD1PHEB 1954.907 -18.526-0.272 1.00 48.32B C

ATOM 3585CD2PHEB 1956.690 -17.6791.088 1.00 49.37B C

ATOM 3586CEtPHEB 1954.001 -17.7060.396 1.00 47.26B C

ATOM 3587CE2PHEB 1955.790 -16.8531.763 1.00 48.25B C

ATOM 3588C2 PHEB 1954.444 -16.8691.415 1.00 47.46B C

ATOM 3589C PHEB 1958.082 -17.512-2.003 1.00 51.70B C

ATOM 3590O PHE. 1957.374 -16.560-2.320 1.00 52.15B O
B

ATOM 3591N ALAI 1969.333 -17.372-1.582 1.00 51.07B N
B

ATOM 3592CA ALAI 1969.952 -16.062-1.480 1.00 50.75B C
B

ATOM 3593CB ALA' 19611.397 -16.2151.062 1.00 49.93B C
B

ATOM 3594C ALAB 1969.863 -15.323-2.816 1.00 51.54B C

ATOM 3595O ALA' 1969.609 -14.119-2.859 1.00 51.65B 0 B

ATOM 3596N SERB 19710.056 -16.055-3.905 1.00 51.42B N

ATOM 3597CA SERB 19710.022 -15.472-5.241 1.00 51.45B C

ATOM 3598CB SERB 19710.520 -16.499-6.270 1.00 51.56B C

ATOM 3599OG SERB 19711.848 -16.916-5.989 1.00 52.33B O

ATOM 3600C SERB 1978.648 -14.956-5.673 1.00 51.35B C

ATOM 36010 SERB 1978.532 -13.864-6.234 1.00 51.47B O

ATOM 3602N ALAB 1987.610 -15.741-5.415 1.00 50.53B N

ATOM 3603CA ALAB 1986.264 -15.365-5.823 1.00 50.56B C

ATOM 3604CB ALAB 1985.331 -16.566-5.682 1.00 50.66B C

ATOM 3605C ALAB 1985.705 -14.164-5.059 1.00 50.08B C

ATOM 3606O ALAB 1984.693 -13.580-5.453 1.00 50.57B 0 ATOM 3607N ILEB 1996.373 -13.788-3.977 1.00 48.34B N

ATOM 3608CA ILEB 1995.922 -12.669-3.164 1.00 45.83B C

ATOM 3609CB ILEB 1995.655 -13.104-1.712 1.00 45.45B C

ATOM 3610CG2ILEB 1994.696 -14.291-1.678 1.00 46.51B C

ATOM 3611CG1ILEB 1996.982 -13.479-1.044 1.00 43.93B C

ATOM 3612CD1ILEB 1996.904 -13.5940.455 1.00 43.22B C

ATOM 3613C ILEB 1996.969 -11.571-3.097 1.00 44.02B C

ATOM 3614O ILEB 1996.700 -10.505-2.561 1.00 43.10B O

ATOM 3615N HiSB 2008.153 -11.831-3.645 1.00 42.58B N

ATOM 3616CA HISB 2009.253 -10.868-3.573 1.00 40.99B C

ATOM 3617CB HISB 20010.474 -11.382-4.361 1.00 38.72B C

ATOM 3618CG HISB 20010.623 -10.792-5.732 1.00 39.33B C

ATOM 3619CD2HISB 20011.427 -9.802-6.192 1.00 38.46B C

ATOM 3620ND1HISB 2009.889 -11.220-6.816 1.00 40.33B N

ATOM 3621CE1HISB 20010.233 -10.520-7.884 1.00 38.85B C

ATOM 3622C HISB 2008.919 -9.430-3.972 1.00 39.97B C

ATOM 3623O HISB 2009.573 -8.498-3.514 1.00 38.23B O

ATOM 3624NE2HISB 20011.163 -9.651-7.531 1.00 39.85B N

ATOM 3625N ASPB 2017.904 -9.240-4.810 1.00 40.33B N

ATOM 3626CA ASPB 2017.533 -7.889-5.217 1.00 41.32B C

ATOM 3627CB ASPB 2017.911 -7.647-6,688 1.00 43.91. C
B

ATOM 3628CG ASPB 2019.347 -7.152-6.864 1.00 44.90B C

ATOM 3629C ASPB 2016.051 -7.556-5.032 1.00 40.63B C

ATOM 3630O ASPB 2015.604 -6.508-5.490 1.00 40.26B O

ATOM 3631OD1ASPB 2019.90_3 -6.568-5.919 1.00 50.28B O

ATOM 3632OD2ASPB 2019.917 -7.330-7.960 1.00 46.89B O

ATOM 3633N VALB 2025.293 -8.422-4.357 1.00 39.38B N

ATOM 3634CA VALB 2023.856 -8.179-4.187 1.00 37.72B C

ATOM 3635CB VALB 2023.174 -9.233-3.227 1.00 37.90B C

ATOM 3636CG1VALB 2023.531 -8.973-1.780 1.00 36.30B C

ATOM 3637CG2VALB 2021.662 -9.193-3.402 1.00 36.87B C

ATOM 3638C VALB 2023.508 -6.773-3.699 1.00 37.34B C

ATOM 3639O VALB 2024.135 -6.241-2.779 1.00 35.77B O

ATOM 3640N ASPB 2032.516 -6.178-4.359 1.00 36.29B N

ATOM 3641CA ASPB 2032.020 -4.854-4.019 1.00 36 B C

12 ATOM 3642CB ASPB 2031.543 -4.852-2.567 1.00 . B C
35.63 ATOM 3643CG ASPB 2030.712 -3.639-2.224 1.00 35.88B C

ATOM 3644OD1ASPB 203-0.197 -3.299-3.011 1.00 35.61B O
ATOM 3645OD2ASPB 2030.960 -3.041-1.155 1.00 35.79B O

ATOM 3646C ASPB 2033.034 -3.741-4.235 1.00 36.28B C

ATOM 3647O ASPB~2033.086 -2.779_ -3.4%01.00 36.97 B O

ATOM 3648N HISB 2043.840 -3.872-5.280 1.00 35.87 B N
' ATOM 3649CA HISB 2044.839 -2.853-5.589 1.00 34.20 B C

ATOM 3650CH H1SB 2045.858 -3.417-6.568 1.00 31.78 B C

ATOM 3651CG HISB 2047.091 -2.586-6.701 1.00 31.61 B C

ATOM 3652CD2HISB 2048.385 -2.863-6.415 1.00 30.89 B C

ATOM 3653ND1HISB 2047.076 -1.313-7.228 1.00 _ B N
30.47 ATOM 3654CE1HISB 2048.309 -0.841-7.264 1.00 31.96 B C

ATOM 3655NE2HISB 2049.122 -1.762-6.777 1.00 33.37 B N

ATOM 3656C HISB 2044.078 -1.684-6.210 1.00 33.61 B C

ATOM 3657O HISB 2043.275 -1.871-7.129 1.00 34.60 B O

ATOM 3658N PROB 2054.319 -0.462-5.720 1.00 32.81 B N

ATOM 3659CD PROB 2055.159 -0.123-4.559 1.00 33.12 B C

ATOM 3660CA PROB 2053.634 0.730 -6.230 1.00 32.80 B C

ATOM 3661CB PROB 2053.784 1.716 -5.077 1.00 32.33 B C

ATOM 3662CG PROB 2055.153 1.403 -4.582 1.00 33.41 B C

ATOM 3663C PROB 2054,124 1.310 -7.550 1.00 32.36 B C

ATOM 3664O PROB 2053.480 2.197 -8.112 1.00 33.25 B O

ATOM 3665N GLYB 2065.254 0.818 -8.044 1.00 31.83 B N

ATOM 3666CA GLYB 2065.788 1.326 -9.294 1.00 31.52 8 C

ATOM 3667C GLYB 2066.809 2.433 -9.097 1.00 31.68 B C

ATOM 36680 GLYB 2067.294 3.018 -10.0661.00 32.94 B 0 ATOM 3669N VALB 2077.142 2.718 -7.843 1.00 30.43 B N

ATOM 3670CA VALB 2078.114 3.761 -7,514 1.00 29.95 B C

ATOM 3671CB VALB 2077.414 4.982 -6.867 1.00 30.12 B C

ATOM 3672CG1VALB 2076.558 5.704 -7.908 1.00 30.73 B C

ATOM 3673CG2VALB 2076.535 4.520 -5.719 1.00 28.12 B C

ATOM 3674C VALB 2079.179 3.220 -6.551 1.00 29.71 B C

ATOM 3675O VALB 2078.926 2.306 -5.769 1.00 29.11 B O

ATOM 3676N SERB 20810.369 3.796 -6.609 1.00 29.44 B N

ATOM 3677CA SERB 20811.480 3.359 -5.764 1.00 29.48 B C

ATOM 3678CB SERB 20812.772 3.974 -6.279 1.00 26.35 B C

ATOM 3679OG SERB 20812.695 5.375 -6:154 1.00 28.20 B O

ATOM 3680C SERB 20811.323 3.720 -4.284 1.00 28.53 B C

ATOM 3681O SERB 20810.478 4.536 -3.918 1.00 28.80 B O

ATOM 3682N ASNB 20912.156 3.118 -3.440 1.00 27.42 B N

ATOM 3683CA ASNB 20912.110 3.401 -2.014 1.00 26.93 B C

ATOM 3684CB ASNB 20913.122 2.533 -1.232 1.00 27.96 B C

ATOM 3685CG ASN' 20912.723 1.062 -1.170 1.00 28.46 B C
B

ATOM 3686OD1ASN, 20911.587 0.730 -0:859 1.00 31.57 B O
B

ATOM 3687ND2ASNB 20913.666 0.177 -1.463 1.00 29.95 8 N

ATOM 3688C ASNB 20912.412 4.872 -1.760 1.00 25.64 B C

ATOM 3689O ASNB 20911.760 5.516 -0.932 1.00 27.11 B O

ATOM 3690N GLNB 21013.404 5.413 -2.459 1.00 24.73 B N

ATOM 3691CA GLNB 21013.765 6.817 -2.255 1.00 23.84 B C

ATOM 3692CB GLNB 21014.971 7.200 -3.126 1.00 23.23 B C

ATOM 3693CG GLNB 21015.605 8.533 -2.739 1.00 26.12 B C

ATOM 3694CD GLNB 21016.166 8.527 -1.318 1.00 30.82 B C

ATOM 3695OE1GLNB 21017.013 7.695 -0.980 1.00 33.39 B O

ATOM 3696NE2GLNB 21015.700 9.454 -0.482 1.00 30.06 B N

ATOM 3697C GLNB 21012.571 7.740 -2.546 1.00 22.80 B C

ATOM 3698O GLNB 21012.387 5.740 -1.882 1.00 23.80 B O

ATOM 3699N PHEB 21111.762 7.397 -3.540 1.00 23.77 B N

ATOM 3700CA PHEB 21110.591 8.196 -3.864 1.00 23.35 B C

ATOM 3701CB PHEB 2119.909 7.668 -5.145 1.00 22.14 B C

ATOM 3702CG PHEB 2118.722 8.500 -5.595 1.00 24.16 B C

ATOM 3703CD1PHEB 2117.461 . 8.306-5.033 1.00 24.44 B C

ATOM 3704CD2PHEB 2118.883 9.524 -6.533 1.00 25.35 B C

ATOM 3705CE1PHEB 2116.382 9.115 -5.391 1.00 24.83 B C

ATOM 3706CE2PHEB 2117.807 10.342-6.896 1.00 26.46 B C

ATOM 3707CZ PHEB 2116.953 10.135-6.320 1.00 25.09 B C

ATOM 3708C PHEB 2119.631 8.129 -2.672 1.00 24.41 B C
ATOM 3709O PHEB 2119.098 9.155 -2.237 1.00 25.60 B O

ATOM 3710N LEUB 2129.419 6.923 -2.144 1.00 23.65 B N
ATOM 3711CA LEUB 2128.544 6.744 -0.997 1.00 23.86 B C
ATOM 3712CB LEUB 2128.360 5.259 -0.675 1.00 23.47 B C
ATOM 3713CG LEUB 212-- 7.6594.412 -1.747 1.00 24.70 B C
ATOM 3714CD1LEUB 2127.483 2.991 -1,240 1.00 23.54 B C
ATOM 3715CD2LEUB 2126.284 5.014 -2.073 1.00 22.98 B C
ATOM 3716C LEUB 2129.125 7.464 0.215 1.00 25.06 B C
ATOM 3717O LEUB 2128.386 8.014 1.044 1.00 25.67 B 0 ATOM 3718N ILEB 21310.449 7.46 7 0.3271.00 24.08 B N
ATOM 3719CA ILEB 21311.094 8.144 1.446 1.00 22.38 B C
ATOM 3720CB ILEB 21312.600 7.757 1.506 1.00 23.24 B C
ATOM 3721CG2ILE8 21313.336 8.736 2.469 1.00 17.99 B C
ATOM 3722CG1ILEB 21312.763 6.296 1.820 1.00 23.89 B C
ATOM 3723CD1ILEB 21314.232 5.811 1.830 1.00 22.53 B C
ATOM 3724C ILEB 21310.971 9.666 1.303 1.00 23.37 B C
ATOM 3725O ILEB 21310.648 10.3722.260 1.00 23.91 B 0 ATOM 3726N ASNB 21411.247 10.1830.107 1.00 23.54 B N
ATOM 3727CA ASNB 21411.196 11.629-0.100 1.00 24.75 B C
ATOM 3728CB ASNB 21411.661 11.990-1.519 1.00 25.98 B C
ATOM 3729CG ASNB 21413.148 11.727-1.729 1.00 30.01 B C
ATOM 3730OD1ASNB 21413.883 11.454-0.772 1.00 30.36 B O
ATOM 3731ND2ASNB 21413.599 11.815-2.977 1.00 28.44 B N
ATOM 3732C ASNB 2149.821 12.2280.183 1.00 23.18 B C

ATOM 3733O ASNB 2149.720 13.3230.703 1.00 22.24 B O

ATOM 3734N THRB 2158.770 11.489-0.1411.00 23.60 B N

ATOM 3735CA THRB 2157.412 11.9590.080 1.00 25.24 B C

ATOM 3736CB THRB 2156.429 11.260-0.9051.00 26.23 B C

ATOM 3737OG1THRB 2156.554 9.831 -0.7801.00 26.09 B O

ATOM 3738CG2THR8 2156.709 11.677-2-3381.00 23.97 B C

ATOM 3739C THRB 2156.867 11.7461.504 1.00 25.71 B C

ATOM 3740O THRB 2155.749 12.1651.791 1.00 26.65 B O

ATOM 3741N ASNB 2167.653 11.1222.385 1.00 25.78 B N

ATOM 3742CA ASNB 2167.224 10.7933.753 1.00 27.36 B C

ATOM 3743CB ASNB 2166.819 12.0074.604 1.00 28.34 B C

ATOM 3744CG ASNB 2167.750 13.1794.442 1.00 29.86 8 C

ATOM 3745ODtASNB 2168.926 13.0164.129 1.00 30.28 B O

ATOM 3746ND2ASNB 216_7.2_2914.3744.670 1.00 29.07 B N

ATOM 3747C ASNB 2166.007 9.903 3.646 1.00 27.48 B C

ATOM 3748O ASNB 2165.041 10.0704.384 1.00 26.81 B O

ATOM 3749N SERB 2176.039 8.966 2.711 1.00 28.78 B N

ATOM 3750CA SERB 2174.920 8.064 2.569 1.00 30.88 B C

ATOM 3751CB SERB 2175.165 7.087 1.427 1.00 31.84 B C

ATOM 3752OG SERB 2176.286 6.279 1.716 1.00 33.36 B O

ATOM 3753C SERB 2174.783 7.290 3.874 1.00 32.55 B C

ATOM 3754O SERB 2175.763 7.101 4.615 1.00 31.95 B O

ATOM 3755N GLUB 2183.561 6.851 4.14'71.00 32.46 8 N

ATOM 3756CA GLUB 2183.256 6.079 5.343 1.00 33.78 B C

ATOM 3757CB GLUB 2181.777 5.686 5.303 1.00 35.91 B C

ATOM 3758CG GLUB 2181.362 4.587 6.255 1.00 39.38 8 C

ATOM 3759CD GLUB 2180.046 3.932 5.841 1.00 42.03 B C

ATOM 3760OE1GLUB 2180.007 3.284 4.764 1.00 42.88 B O

ATOM 3761OE2GLUB 218-0.943 4.066 6.595 1.00 41.04 B O

ATOM 3762C GLUB 2184.136 4.824 5.434 1.00 32.91 B C

ATOM 3763O GLUB 2184.598 4.448 6:512 1.00 33.32 B O

ATOM 3764N LEU~ 2194.361 4.187 4.291 1.00 32.05 B N
B

ATOM 3765CA LEUB 2195.154 2.966 4.211 1.00 31.69 B C

ATOM 3766CB LEUB 2195.100 2.430 2.775 1.00 31.69 B C

ATOM 3767CG LEU. 2194.871 0.935 2.517 1.00 34.70 B C
B

ATOM 3768CD1LEUB 2193.972 0.311 3.593 1.00 35.20 B C

ATOM 3769CD2LEUB 2194.243 0.766 9.138 1.00 33.48 B C

ATOM 3770C LEUB 2196.599 3.205 4.649 1.00 30.48 B C

ATOM 3771O LEUB 2197.222 2.347 5.271 1.00 29.40 B O

ATOM 3772N ALAB 2207.123 4.383 4.340 1.00 29.35 B N

ATOM 3773CA ALAB 2208.495 4.712 4.707 1.00 29.86 B C

ATOM 3774OB ALAB 2209.027 5.861 3.818 1.00 27.86 B C

ATOM 3775C ALAB 2208.589 5.078 6.190 1.00 29.67 B C

ATOM 3776O ALAB 2209.601 4.811 6.831 1.0D 29.25 B 0 ATOM 3777N LEUB 2217.542 5.698 6.729 1.0D 29.98 B N

ATOM 3778CA LEUB 2217.514 6.061 8.148 1.00 29.95 B C

ATOM 3779CB LEUB 2216.327 6.982 8.450 1.00 32.33 B C

ATOM 3780CG LEUB 2216.453 8.417 7.931 1.00 36.68 B C

ATOM 3781CD1LEUB 2215.122 9.141 8.060 1.00 39.21 B C

ATOM 3782CD2LEUB 2217.546 9.140 8.712 1.00 39.48 B C
ATOM 3783C LEUB 2217.385 4.778 8.975 1.00 29.65 B C
ATOM 3784O LEUB 2217.914 4.675 10.0901.00 28.37 B O

ATOM 3785N METB 2226.684 3.798 8.424 1.00 28.02 B N
ATOM 3786CA METB 2226.508 2.543 9.128 1.00 30.95 B C
ATOM 3787CB METB 2225.432 1.702 8.448 1.00 33.52 B C

ATOM 3788CG METB 2225.340 0.281 8.973 1.00 38.61 B C
ATOM 3789SD METB 2225.084 0.233 10.7791.00 47,44 B S
ATOM 3790CE METB 2223.297 0.728 10.8631.00 44.25 B C
ATOM 3791C METB 2227.793 1.720 9.223 1.00 30.43 B C
ATOM 3792O METB 2228.040 1.089 10.2451.00 30.12 B O
ATOM 3793N TYRB 2238.603 1.736 8.164 1.00 29.67 B N
ATOM 3794CA TYRB 2239.834 0.950 8.117 1.00 28.66 B C
ATOM 3795CB TYRB 2239.870 0.132 6.827 1.00 27.00 B C
ATOM 3796CG TYRB 2238.810 -0.9556.787 1.00 26.12 B C
ATOM 3797CD1TYRB 2238.811 -2.0017.722 1.00 26.66 B C
ATOM 3798CE1TYRB 2237.801 -2.9717.725 1.00 27.65 B C
ATOM 3799CD2TYRB 2237.783 -0.9145.853 1.00 28.11 B C
ATOM 3800CE2TYRB 2236.772 -1.8765.838 1.00 28.18 B C
ATOM 3801CZ TYRB 2236.781 -2.8976.774 1.00 29.59 B C
ATOM 3802OH TYRB 2235.760 -3.8276.755 1.00 32.47 B O
ATOM 3803C TYRB 22311.122 1.732 8.270 1.00 28.67 B C
ATOM 38040 TYRB 22312.202 1.223 8.004 1.00 30,91 B O
ATOM 3805N ASNB 22411.006 2.975 8.700 1.00 29.40 B N
ATOM 3806CA ASNB 22412.171 3.822 8.925 1.00 29.37 B C
ATOM 3807CB ASNB 22412.895 3.319 10.1821.00 28.48 B C
ATOM 3808CG ASNB 22411.987 3.324 11.4011.00 27.15 B C
ATOM 3809OD1ASNB 22411.510 4.376 11.8151.00 26.61 B O
ATOM 3810ND2ASNB 22411.728 2.146 11.9681.00 25.87 B N
ATOM 3811C ASNB 22413.156 3.993 7.760 1.00 29.58 B C
ATOM 3812O ASNB 22414.372 3.910 7.948 1.00 28.26 B O
ATOM 3813N ASPB 22512.621 4.238 6.565 1.00 29.59 B N
ATOM 3814CA ASPB 22513.430 4.473 5.350 1,00 30.98 B C
ATOM 3815CB ASPB 22514.219 5.798 5.476 1.00 29.43 B C
ATOM 3816CG ASPB 22513.313 7.028 5.692 1.00 28.82 B C
ATOM 3817OD1ASPB 22512.148 7.023 5.259 1.00 28.85 B O
ATOM 3818OD2ASPB 22513.775 8.019 6.284 1.00 25.81 B O

ATOM 3819C ASPB 22514.415 3.350 _ 4.9851.00 B C
ATOM 3820O ASPB 22515.308 3.54 0 _ 33.03 B O
ATOM 3821N SERB 22614.241 2.178 4.148 1.00 B N
ATOM 3822CA SERB 22615.146 1.066 5.590 33.98 B C
ATOM 3823CB SERB 22615.801 0.651 5.344 1.00 B C
ATOM 3824OG SERB 22616.342 1.786 6.668 33.46 B O
ATOM 3825C SERB 22614.418 -0.1147.349 1.00 B C
ATOM 3826O SERB 22613.525 -0.6824.718 32.95 B O
ATOM 3827N SERB 22714.803 -0.4745.333 1.00 B N
ATOM 3828CA SERB 22714.181 -1.5823.493 34.44 B C
ATOM 3829CB SERB 22714.624 -2.9222.779 1.00 B C
ATOM 3830OG SERB 22716.012 -3.1213.373 32.67 B O
ATOM 3831C SERB 22712.664 -1.4833.192 1.00 B C
ATOM 3832O SERB 22711.962 -2.4922.837 33.79 B O
ATOM 3833N VALB 22812.170 -0.2592.986 1.00 B N
2.701 33.56 1.00 33.38 1.00 33.85 1,00 34.35 1.00 34.95 1.00 34.61 1.00 34.94 1.00 34.20 ATOM 3834CA VALB 22810:745 0.024 2.752 1.00 32.47 B C

ATOM 3835CB VALB 22810.496 1.464 2.292 1.00 32.22 B C

ATOM 3836CG1VALB 2289.005 1.770 2.272 1.00 32.42 B C

ATOM 3837CG2VALB 22811.228 2.422 3 1 30 B C

ATOM 3838C VALB 2289.884 -0.939. . . B C
1.947 1.00 33.13 ATOM 3839O VALB 2288.988 -1.6032.486 1.00 33.74 B O

ATOM 3840N LEUB 22910.150 -1.0260.654 1.00 33.06 B N

ATOM 3841CA LEUB 2299.371 -1.906-0.194 1.00 32.50 B C

ATOM 3842CB LEUB 2299.667 -1.606-1.661 1.00 31,50 B C

ATOM 3843CG LEUB 2298.869 -0.424-2 1 31 B C

ATOM 3844CD1LEUB 2299.300 -0.114. . . B C
-3.638 1.00 33.08 ATOM 3845CD2LEUB 2297.379 -0.765-2.145 1.00 30.65 B C

ATOM 3846C LEUB 2299.587 -3.3840.103 1.00 33.61 B C

ATOM 3847O LEUB 2298.637 -4.1720.077 1 34 B O

ATOM 3848N GLUB 23010.825 -3.7670 . . B N

ATOM 3849CA GLUB 23011.124 -5.167. . . B C
0.694 1.00 33.65 ATOM 3850CB GLUB 23012.633 -5.3710.821 1.00 32.83 B C

ATOM 3851CG GLUB 23013.403 -5.172-0 1 33 B C

ATOM 3852CD GLUB 23013.405 -3.733. . . B C
-0.961 1.00 33.50 ATOM 3853OE1GLUB 23013.110 -2.825-0.151 1.00 33.12 B O

ATOM 3854OE2GLUB 23013.721 -3.513-2 1 34 B O

ATOM 3855C GLUB 23010.426 -5.627. . . B C
1.970 1.00 33.41 ATOM 3856O GLUB 2309.932 -6.7472.045 1.00 32.71 B 0 ATOM 3557N ASNB 23110.398 -4.7652.982 1.00 34.88 B N

ATOM 3858CA ASNB 2319.730 -5.1134.225 1.00 35.53 B C

ATOM 3859CB ASNB 2319.934 -4.0295.279 1 34 B C

ATOM 3860CG ASNB 23111,191 -4.2446 . . B

. . , C
ATOM 3861OD1ASN; 23111.392 -5.3116.646 1.00 34 B O
. B 69 ATOM 3862ND2ASNI 23112.041 -3.2316.163 1.00 . B N
B 34.14 ATOM 3863C ASNB 2318.254 -5.2763.928 1.00 36.44 B C

ATOM 3864O ASNB 2317.614 -6.2174.404 1.00 36.98 B O

ATOM 3865N HISB 2327.725 -4.3713 1 36 B N

ATOM 3866CA HISB 2326.316 -4.410. . . B

. . . C
ATOM 3867CB HISB 2325.938 -3 1 1 . . . 36.82 B C

. . . 1.00 37.14 B C

. -2.9140.469 1.00 37.58 B C

ATOM 3870ND1HISB 2323.519 -3.1192.626 1 38 B N

ATOM 3871CE1HISB 2322.323 -2 2 . .

. . . 37.45 B C

. . . 1.00 38.24 B N
ATOM 3873C HISB 2325.997 -5 1 1 . , .00 38.46 B C

. . 2.229 1.00 38.71 B O
ATOM

3875N HISB 2336.851 -5.9890.999 1.00 38 B N

ATOM 3876CA HISB 2336.649 -7.1860.188 1.00 . B C
39.05 ATOM 3877CB HISB 2337.845 -7.416-0.738 1 38 B C

ATOM 3878CG HiSB 2338.028 -6.338-1 . .

. . .40 B C
ATOM 3879CD2HISB 2339.139 -5 -2 . . 1.00 35.22 B C
ATOM 3880NDiHISB 2336 -5 . . -2.481 1.00 35.59 B N

7.435 -4.886-3.301 1.00 35.68 B C

ATOM 3882NE2HISB 2338.742 -4,789-3.137 1 35 B N

ATOM 3883C HISB 2336.450 -8 1 . .

. . 1.00 39.72 B C

. . 0.930 1.00 39.52 B O

7.370 -8.582~ 2.0371.00 39.49 B N

ATOM 3886CA LEUB 2347.286 -9.6882.980 1 41 B

. . C
ATOM 3887CB LEUB 2348.470 -9 3 . . 1.00 41.48 B C
ATOM 3888CG LEUB 2349.798 -10 3 . . 1.00 42.29 B C

. . 4.327 1.00 42.94 B C

. -11.6013.094 1.00 43.60 B C

ATOM 3891C LEUB 2345.974 -9.6453 1 43 B

. . . C
ATOM 3892O LEUB 2345.196 -10 3 . . 1.00 41.62 B O

. . 4.453 1.00 44.63 B N

. -8.3175.269 1.00 45.94 B C

5 4.500 -6.5795.772 1.00 46.68 B C

ATOM 3896C ALAB 2353.234 -8.6544 1 46 . . . B C

. . . 1.00 48.03 B O

. -8.3603.278 1.00 47,02 B N

OM 3899CA VALB 2361.923 -8.6622.537 1 47 B C

ATOM 3900CB VALB 2361.792 -7.7881 . .

. . 45.86 B C
ATOM 3901CG1VALB 2360.640 -8 0 . . 1.00 44.26 B C

. . 1.675 1.00 46.59 B C

. -10.1232.125 1.00 48.69 B C

M 3904O VALB 2360.902 -10 1 1 . . , 48.54 B O

ATOM 3905N GLYB 2373.147 -10.6461.906 1,00 49.79 B N

ATOM 3906CA GLYB 2373.270 -12.0371.523 1.00 51.17 B C

ATOM 3907C GLYB 2372.719 -12.9242:620 1.00 51.91 B C

ATOM 3908O GLYB 2371.971 -13.8662.360 1.00 51.26 B O

ATOM 3909N PHEB 2383.086 -12.6143.857 1.00 53.16 B N

ATOM 3910CA PHEB 2382.624 -13.3894.994 1.00 55.58 B C

ATOM 3911CB PHEB 2383.501 -13.1076.208 1.00 55.62 B C

ATOM 3912CG PHEB 2384.922 -13.5426.032 1.00 56.15 B C

ATOM 3913CD1PHEB 2385.219 -14.8615.700 1.00 56.34 B C

ATOM 3914CD2PHEB 2385.968 -12.6436.210 1.00 55.97 B C

ATOM 3915CE1PHEB 2386.538 -15.2835.549 1.00 56.52 B C

ATOM 3916CE2PHEB 2387.291 -13.0516.062 1.00 56.16 B C
_ ATOM 3917CZ PHEB 2387.577 -14.3785.731 1.00 56.81 B C

ATOM 3918C PHEB 2381.172 -13.0695.304 1.00 57.30 B C

ATOM 3919O PH B 238E -13.9325.176 1.00 58.32 B 0 0.302 ATOM 3920N LYSB 2390.906 -11.8295:698 1:00 58.07 B N

ATOM 3921CA LYSB 239-0.456 -11.4226.015 1.00 58.95 B C

ATOM 3922CB LYSB 239-0.558 -9.8946.046 1.00 59.69 B C

ATOM 3923CG LYSB 239-1.919 -9.3556.481 1.D0 60.94 B C

ATOM 3924CD LYSB 239-2.260 -9.7117.933 1.00 61.68 B C

ATOM 3925CE LYSB 2393.660 -9.2208.301 1.00 62.30 B C

ATOM 3926NZ LYSB 239-4.103 -9.6369.661 1.00 62.86 B N

ATOM 3927C LYS8 239.-1.471 -11.9965.020 1.00 58.85 B C

ATOM 3928O LYS~ 239-2.567 -12.3895.408 1.00 59.82 B O
B

ATOM 3929N LEUB 240-1.115 -12.0623.741 1.00 58.58 B N

ATOM 3930CA LEUi 240-2.051 -12.5992.757 1.00 58.97 B C
B

ATOM 3931CB LEUB 240-1.536 -12.3851.328 1.00 57.92 B C

ATOM 3932CG LEUB 240-1.758 -10.9930.717 1.00 57.71 B C

ATOM 3933CDtLEUB 240-1.385 -11.027-0.7561.00 56.33 B C

ATOM 3934CD2LEUB 240-3.221 -10.5710.874 1.00 56.63 B C

ATOM 3935C LEUB 240-2.359 -14.0762.979 1.00 60.31 B C

ATOM 3936O LEUB 240-3.262 -14.6312.343 1.00 59.86 B O

ATOM 3937N LEUB 241-1.601 -14.7133.872 1.00 61.21 B N

ATOM 3938CA LEUB 241-1.816 -16.1214.195 1.00 61.96 B C

ATOM 3939CB LEUB 241-0.620 -16.6934.967 1.00 61.08 B C

ATOM 3940CG LEUB 2410.698 -16.9284.216 1.00 60.70 B C

ATOM 3941CD1LEUB 2411.757 -17.4245.186 1.00 60.74 B C

ATOM 3942CD2LEUB 2410.494 -17.9423.108 1,00 60.43 B C

ATOM 3943C LEUB 241-3.076 -16.2265.055 1.00 62.91 B C

ATOM 3944O LEUB 241-3.867 -17.1614.915 1.00 62.76 B O

ATOM 3945N GLNB 242-3.255 -15.2375.925 1.00 63.89 B N

ATOM 3946CA GLNB 242-4.389 -15.1626.838 1.00 64.74 B C

ATOM 3947CB GLNB 242-4.116 -14.0867.884 1.00 64.63 B C

ATOM 3948CG GLNB 242-2.869 -14.3328.702 1.00 64.56 B C

ATOM 3949CD GLNB 242-2.450 -13.1139.498 1.00 64.90 B C

ATOM 3950OE1GLNB 242-3.286 -12.41610.0731.00 64.62 B 0 ATOM 3951NE2GLNB 242-1.144 -12.8559.546 1.00 65.09 B N

ATOM 3952C GLNB 242-5.742 -14.8796.180 1.00 66.04 B C

ATOM 3953O GLNB 242-6.760 -14.8316.868 1.00 66.34 B 0 ATOM 3954N GLUB 243-5.762 -14.6834.864 1.00 67.78 B N

ATOM 3955CA GLUB 243-7.018 -14.4054.160 1.00 69.37 B C

ATOM 3956CB GLUB 243-6.766 -14.1692.664 1.00 69.49 B C

ATOM 3957CG GLUB 243-6.031 -12.8812.323 1.00 69.26 B C

ATOM 3958CD GLUB 243-0.959 -11.7621.885 1.00 68.94 B C

ATOM 3959OE1GLUB 243-7.691 -11,9490.890 1.00 67.58 B O

ATOM 3960OE2GLUB 243-6.945 -10.6912.530 1.00 69.31 B O

ATOM 3961C GLUB 243-7.989 -15.5704.328 1.00 70.13 B C
ATOM 3962O GLUB 243-7.976 -16.2545.349 1.00 70.62 B O
ATOM 3963N GLUB 244-8.825 -15.7973.321 1.00 70.84 B N

ATOM 3964CA GLUB 244-9.794 -16.8843.372 1.00 71.91 B C
ATOM 3965CB GLUB 244-11.106-16.4512.705 1,00 72 B C

ATOM 3966CG GLUB 244-12.147-17.5592.521 1.00 . B C
ATOM 3967CD GLUB 244-12.368-18.4063.769 1.00 72.66 B C
72.87 ATOM 3968OE1GLUB 244-12.159-17.9034.895 1.00 73.51 B O
ATOM 3969OE2GLUB 244-12.770-19.5773.620 1.00 72.25 B O
ATOM 3970C GLUB 244-9.249 -18.1292.693 1.00 72.36 B C
ATOM 3971O GLUB 244-9,108 -18.1671.469 1.00 72.63 B 0 ATOM 3972N ASNB 245-8.943 -19.1433.499 1,00 72.70 B N
ATOM 3973CA ASNB 245-8.413 -20.4072.995 1.00 73.15 B C
ATOM 3974CB ASNB 245-9.496 -21.1652.225 1.00 73.13 B C
ATOM 3975CG ASNB 245-9.099 -22.6001.923 1.00 73.58 B C
ATOM 3976OD1ASNB 245-9.660 -23.2351.D29 1.00 73.38 B 0 ATOM 3977ND2ASNB 245-8.136 -23.1212.679 1.00 73.12 B N
ATOM 3978C ASNB 245-7.211 -20.1772.081 1.00 73.17 B C
ATOM 3979O ASNB 245-7.237 ' -20.5310.900 1.00 72.50 B O
ATOM 3980N CYSB 246-6.157 -19.5872.635 1.00 74.04 B N
ATOM 3981CA CYSB 246-4.950 -19.3021.868 1.00 74.48 B C
ATOM 3982CB CYSB 246-4.868 -17.8061.551 1.00 74.46 B C
ATOM 3983SG CYSB 246-6.253 -17.1540.586 1.00 74.07 B S
ATOM 3984C CYSB 246-3.705 -19.7202.631 1.00 74.92 B C
ATOM 3985O CYSB 246-2.600 -19.6902.086 1.00 74.71 B O
ATOM 3986N ASPB 247-3.892 -20.1083.891 1.00 75.74 B N
ATOM 3987CA ASP8 247-2.786 -20.5224.754 1.00 76.64 B C
ATOM 3988CB ASPB 247-3.260 -20.6106.206 1.00 76.96 B C
ATOM 3989CG ASPB 247-2.139 -20.3797.204 1.D0 77.gg g C
ATOM 3990OD1ASPB 247-1.074 -21.0237.072 1.00 78.19 B O

ATOM 3991OD2ASPB 247-2.328 -19.5528.125 ' 1.0078.03 B O

ATOM 3992C ASPB 247-2.241 -21.8754.314 1.00 77.12 B C

ATOM 3993O ASPB 247-2.505 -22.8954.947 1.0D 77.30 B O

ATOM 3994N ILEB 248-1.478 -21.8773.228 1.00 77.61 B N

ATOM 3995CA ILEB 248-0.912 -23.1072.695 1.00 78.03 B C

ATOM 3996CB ILEB 248-0.104 -22.8281.401 1.00 77.72 B C

ATOM 3997CG2ILEB 248-1.051 -22.4280.277 1.00 77.07 B C

ATOM 3998CG1ILEB 2480.925 -21.7221.646 1.00 77.66 B C

ATOM 3999CD1ILEB 2481.701 -21.3180.404 1.00 77.70 B C

ATOM 4000C ILEB 248-0.037 -23.8623.695 1.00 78.52 B C

ATOM 4001O ILEB 248-0.185 -25.0713,856 1.00 79.22 B O

ATOM 4002N PHEB 2490.857 -23.1574.380 1.00 78.65 B N

ATOM 4003CA PHEB 2491.742 -23.8065.342 1.00 79.20 B C

ATOM 4004CB PHEB 2492.883 -22.8645.733 1.00 79.23 B C

ATOM 4005CG PHEB 2493.492 -22.1254.575 1.00 79.26 B C

ATOM 4006CD1PHEB 2493.801 -22.7843.392 1.00 79.24 B C

ATOM 4007CD2PHEB 2493.775 -20.7664.678 1.00 79.25 B C

ATOM 4008CE1PHEB 2494.383 -22.1012.328 1.00 79.46 B C

ATOM 4009CE2PH B 2494.355 -20.0753.622 1.00 79.23 B C

ATOM 4010CZ PHEB 2494.661 -20.7442.444 1.00 79.36 B C

ATOM 4011C PHEB 2491.010 -24.2526.607 1.00 79.74 B C

ATOM 4012O PHEB 2491.589 -24.2627.697 1.00 79.48 B O

ATOM 4013N GLNB 250-0.256 -24.6356.464 1.0D 80.44 B N

ATOM 4014CA GLNB 250-1.055 -25.0567.613 1.00 81.61 B C

ATOM 4015CB GLN8 250-2.549 -24.9877.273 1.00 81.61 B C

ATOM 4016CG GLNB 250-3.003 -26.0116.246 1.00 82 B C

ATOM 4017CD GLNB 250-4.418 -25.7595.758 1.00 . B C
83.45 ATOM 4018OE1GLNB 250-4.664 -24.8364.977 1.00 84.20 B O

ATOM 4019NE2GLNB 250-5.358 -26.5736.225 1.00 83.16 B N

ATOM 4020C GLNB 250-0.708 -26.4608.099 1.00 81.96 B C

ATOM 4021O GLNB 250-0.966 -26.8099.254 1.00 82.05 B O

ATOM 4022N ASNB 251-0.121 -27.2647.220 1.00 82,31 B N

ATOM 4023CA ASNB 2510.236 -28.6237.590 1.00 82.43 B C

ATOM 4024CB ASNB 251-0.226 -29.5996.506 1.00 82.67 B C

ATOM 4025CG ASNB 251-1.738 -29.6956.422 1.00 82.77 B C

ATOM 4026OD1ASNB 251-2.423 -29.7547.443 1.00 83.19 B O

ATOM 4027ND2ASNB 251-2.265 -29.7255.206 1.00 82.95 B N

ATOM 4028C ASNB 2511.720 -28.8167.883 1.00 82.59 B C

ATOM 4029O ASNB 2512.272 -29.8957.668 1.00 82,90 B O

ATOM 4030N LEUB 2522.361 -27.7648.375 1.00 82.36 B N

ATOM 4031CA LEUB 2523.771 -27.8308 1 82 B C

ATOM 4032CB LEUB 2524.556 -26.674. . . B

. . . C
ATOM 4033CG LEUB 2524.877 -26.7546 1 81 B

. . . C
ATOM 4034CD1LEU8 2523.595 -26 5 1 80 . . . .86 B C

. . . 1.00 81.12 B C
ATOM 4036C LEUB 2523.862 -27.74810.251 1.00 82.44 B C

ATOM 4037O LEUB 2522.900 -27.35710.911 1 82 B O

ATOM 4038N THRB 2535.010 -28.11510.806 . . B N
1.00 82.42 ATOM 4039CA THRB 2535.190 -28.07612.253 1.00 82.57 B C

ATOM 4040CB THRB 2536.236 -29.11712 1 83 B C

ATOM 4041OG1THRB 2537.518 -28.793. . . B O
12.161 1.00 83.91 ATOM 4042CG2THRB 2535.830 -30.51412 1 83 B C

ATOM 4043C THRB 2535.633 -26.699. . . B C

ATOM 4044O THRB 2536.054 -25.856. . .

. , . B O
ATOM 4045N LYSB 2545.531 -26.48214 1 81 . . . B N
ATOM 4046CA LYSB 2545.935 -25 14 1 0 . . . .57 B C
ATOM 4047CB LYSB 2545.617 -25 16 1 8 . . . 1. B C
ATOM 4048CG LYSB 2546.221 -24 16 1 2 . . . 82.32 B C
ATOM 4049CD LYSB 2545:764 -22 16 1 . . . 83.66 B C

. . . 1.00 84.35 B C

. . . 1.00 84.06 B N
ATOM 4052C LYSB 2547.431 . 14.450 1.00 80 B C
-25.013 11 ATOM 4053O LYSB 2547.959 -23.92814 1 , B O

ATOM 4054N LYSB 2558.109 -26.063. . . B N

13.999 1 78 ATOM 4055CA LYSB 2559.545 -26 13 . .

. . . 77.22 B C

. . . 1.00 77.54 B C
ATOM 4057CG LYSB 2559.776 -27 15 . . 1.00 78.20 B C
ATOM 4058CD LYSB 25510.269 -29 15 1 . . .00 79.24 B C

. . . 1.00 79.67 B C

. . . 1.00 79.20 B N

. -25.71512.306 1.00 75.57 B C

ATOM 4062O LYSB 25510.770 -25.00811 1 74 B

. . . O
ATOM 4063N GLN8 2568.991 -26 11 . . 1.00 74.18 B N

. . . 1.00 73.07 B C

. . 9.233 1.00 73.33 B C

. -28.4379:378 1.00 73.61 B C

ATOM 4067CD GLNB 2567.430 -29.2658.534 1 74 8 C

ATOM 4068OE1GLNB 2566.216 -29 8 . .

. . . 73.85 B O

. . .579 1.00 73.82 B N

. - 9.737 1.00 72.55 g C
AT 4,585 OM 40710 GLNB 2569.673 -23.8209.283 1 72 B O

ATOM 4072N ARGB 2577.577 -24 10 . .

. . 1.00 71.57 B N

. . 9.824 1.00 69.76 B C

5.744 -22.64110.488 1.00 70.09 B C

ATOM 4075CG ARGB 2574.599 -23.2829.717 1 71 B C

ATOM 4076CD ARGB 2573 -22 . .

. . 10.289 1.00 74.21 B C

ATOM 4077NE ARGB 2572.951 -23.59511-569 1.00 76.31 B N
ATOM 4078CZ ARGB 2573.409 -23.17712.748 1.00 77.60 B C
ATOM 4079NH1ARGB 2574.165 -22.09012.828 1.00 78.45 B N
ATOM 4080NH2ARGB 2573.116 -23.85413.853 1.00 78.02 B N

ATOM 4081C ARGB 2578.081 -21.77510.296 1.00 68.28 B C
ATOM 4082O ARGB 2578.172 -20.7199.678 1.00 68.17 B O
ATOM 4083N GLNB 2588.809 -22.03911.377 1.00 66.66 B N
ATOM 4084CA GLNB 2589.772 -21.05911.878 1.00 65.92 B C
ATOM 4085CB GLNB 25810.205 -21.38413.314 1.00 66.66 B C
ATOM 4086CG GLNB 2589.067 -21.41114.328 1.00 69.42 B C
ATOM 4087CD GLNB 2589.554 -21.46215.774 1.00 70.92 B C
ATOM 4088OE1GLNB 2589.879 -20.42916.373 1.00 71.57 B 0 ATOM 4089NE2GLNB 2589.617 -22.66716.336 1.00 71.26 B N
ATOM 4090C GLNB 25810.999 -21.02310.975 1.00 64.78 B C
ATOM 4091O GLNB 25811.631 -19.97910.804 1.00 64.31 B O
ATOM 4092N SERB 25911.333 -22.17110.396 1.00 63.62 B N
ATOM 4093CA SERB 25912.480 -22.2549.512 1.00 61.95 B C
ATOM 4094CB SERB 25912.846 -23.7159.257 1.00 62.10 B C
ATOM 4095OG SERB 25914.067 -23.8008.544 1.00 62.03 B O
ATOM 4096C SERB 25912.144 -21.5568.198 1.00 60.74 B C
ATOM 4097O SERB 25912.871 -20.6617.757 1.00 59.49 B O
ATOM 4098N LEUB 26011.040 -21.9687.579 1.00 59.73 B N
ATOM 4099CA LEUB 26010.598 -21.3676.322 1.00 59.69 B C
ATOM 4100CB LEUB 2609.215 -21.8935.921 1.00 59.59 B C
ATOM 4101CG LEUB 2608.622 -21.3494.613 1.00 60.13 B C
ATOM 4102CD1LEUB 2609.319 -21.9823.426 1.00 59.72 B C
ATOM 4103CD2LEUB 2607.139 -21.6594.547 1.00 60.71 B C
ATOM 4104C LEUB 26010.531 -19.8516.498 1.00 59.46 B C
ATOM 41050 LEUB 26011.208 -19.1075.787 1.00 60.42 B O
ATOM 4106N ARGB 2619.723 -19.3997.454 1.00 57.90 B N
ATOM 4107CA ARGB 2619.584 -17.9707.710 1.00 56.72 B C
ATOM 4108CB ARGB 2618.903 -17.7129.056 1.00 56.09 B C
ATOM 4109CG ARGB 2618.884 -16.2349.439 1.00 54.13 B C
ATOM 4110CD ARGB 2618.264 -15.98510.805 1.00 53.46 B C
ATOM 4111NE ARGB 2618.382 -14,58511.179 1.00 50.65 B N
ATOM 4112CZ ARGB 2617.712 -13.59810.594 1.00 51.97 B C
ATOM 4113NH1ARGB 2616.862 -13.8609.607 1.00 49.07 B N
ATOM 4114NH2ARGB 2617.918 -12.34610.977 1.00 49.70 B N
ATOM 4115C ARGB 26110.922 -17.2437.694 1.00 55.82 B C
ATOM 4116O ARGB 26111.095 -16.2896.946 1.00 56.31 B O
ATOM 4117N LYSB 26211.867 -17.6848.518 1.00 55.11 B N
ATOM 4118CA LYSB 26213.165 -17.0258.563 1.00 54,84 B C
ATOM 4119CB LYS; 26214.070 -17.6509.628 1,00 54.66 B C
ATOM 4120CG LYSB 26215.456 -17.0099.673 1.00 54.21 B C
ATOM 4121CD LYS' 26216.263 -17.46610.867 1.00 54.38 B C
ATOM 4122CE LYSB 26217.667 -16.88310.832 1.00 54.53 B C
ATOM 4123NZ LYSB 26217.653 -15.39910.718 1.00 55.83 B N
ATOM 4124C LYSB 26213.879 -17.0587.220 1.00 54.75 B C
ATOM 4125O LYSB 26214.619 -16.1326.884 1.00 54.33 B O
ATOM 4126N METB 26313.659 -18:1166.448 1.00 54.41 B N
ATOM 4127CA METB 26314.310 -18.2175.152 1.00 54.18 B C
ATOM 4128CB METB 26314.277 -19.6624.643 1.00 54.48 B C
ATOM 4129CG METB 26315.136 -20.6155.471 1.00 55.84 B C
ATOM 4130SD METB 26315.399 -22.2004.661 1.00 56.49 B S
ATOM 4131CE METB 26313.767 -22.9304.765 1.00 56.92 B C
ATOM 4132C METB 26313.687 -17.2744.128 1.00 53.25 B C
ATOM 41330 METB 26314.399 -16.6133.370 1.00 52.40 B O
ATOM 4134N VALB 26412.361 -17.2044.115 1.00 51.86 B N
ATOM 4135CA VALB 26411.663 -16.3293.185 1.00 51.27 B C
ATOM 4136CB VAL8 26410.136 -16.4733.324 1.00 51.39 B C
ATOM 4137CG1VALB 2649.430 -15.3752.537 1.00 51.74 B C
ATOM 4138CG2VALB 2649.704 -17.8442.813 1.00 51.62 B C
ATOM 4139C VALB 26412.050 -14.8773.425 1.00 50.29 B C
ATOM 4140O VALB 26412.331 -14.1412.488 1.00 50.35 B O
ATOM 4141N ILEB 26512.067 -14.4744.688 1.00 49.87 B N
ATOM 4142CA ILEB 26512.424 -13.1125.058 1.00 48.65 B C
ATOM 4143CB ILEB 26512.288 -12.9066.576 1.00 47.96 B C
ATOM 4144CG2ILEB 26512.843 -11.5416.968 1.00 47.67 B C
ATOM 4145CG1ILEB 26510.820 -13.0626.988 1.00 47.51 B C
ATOM 4146CD1ILEB 26510.594 -13.0088.483 1.00 47.32 B C
ATOM 4147C ILEB 26513.861 -12.8004.651 1.00 48.67 B C
ATOM 4148O ILEB 26514.157 -11.7064.162 1.00 47.53 B O
ATOM 4149N ASPB 26614.751 -13.7654.871 1.00 48.64 B N
ATOM 4150CA ASPB 26616.167 -13.6154.537 1.00 48.54 B C
ATOM 4151CB ASPB 26616.944 -14.8505.006 1.00 49.92 B C
ATOM 4152CG ASPB 26617.354 -14.7676.467 1.00 50.87 B C
ATOM 4153OD1ASPB 26617.685 -15.8247.052 1.00 51.85 B 0 ATOM 4154OD2ASPB 26617.362 -13.6477.027 1.00 51.18 B O
ATOM 4155C ASPB 26616.355 -13.4343.036 1.00 47.09 B C
ATOM 41560 ASPB 26617.183 -12.6412.583 1,00 46.52 B 0 ATOM 4157N ILEB 26715.564 -14.1722.273 1.00 45.77 B N
ATOM 4158CA ILEB 26715.633 -14.1220.827 1.00 44.99 B C
ATOM 4159CB ILEB 26714.845 -15.3190.218 1.00 44.29 B C
ATOM 4160CG2ILEB 26714.712 -15.177-1.299 1.00 42.64 B C
ATOM 4161CG1ILEB 26715.558 -16.6270.581 1.00 44.85 B C
ATOM 4162CD1ILEB 26714.812 -17.8990.148 1.00 45.10 B C
B
B

ATOM 4163C ILEB 26715.110-12.7920.272 1.00 45.10 B C

ATOM 4164O ILEB 26715.846-12.052-0.3791.00 44.44 B O

ATOM 4165N VALB 26813.844-12.4910.541 1.00 44.43 B N

ATOM 4166CA VALB 26813.214-11.2710.053 1.00 43.79 B C
ATOM 4167CB VAL8 26811.788-11.1400.605 1.00 44.59 B C

ATOM 4168CG1VALB 26811.144-9.849 0.094 1.00 43.75 B C

ATOM 4169CG2VALB 26810.965-12.3730.211 1.00 42.73 B C

ATOM 4170C VALB 26813.973-9.989 0.375 1.00 44.65 B C

ATOM 4171O VALB 26814.048-9.088 -0.4631.00 44.29 B 0 ATOM 4172N LEUB 26914.531-9.898 1.581 1.00 44.57 B N

ATOM 4173CA LEUB 26915.270-8.707 1.980 1.00 44.94 B C

ATOM 4174CB LEUB 26915.512-8.699 3.489 1.00 44.76 B C

ATOM 4175CG LEUB 26914.294-8.506 4.402 1.00 46.24 8 C

ATOM 4176CD1LEUB 26914.765-8.379 5.848 1.00 44.54 B C

ATOM 4177CD2LEUB 26913.517-7.264 3.990 1.00 45.38 B C

ATOM 4178C LEUB 26916.602-8.637 1.261 1.00 45.66 B C

ATOM 4179O LEUB 26917.271-7.603 1.259 1.00 46.15 B O

ATOM 4180N ALAB 27016.985-9.754 0.657 1.00 46.22 B N

ATOM 4181CA ALAB 27018.243-9.839 -0.0641.00 46.59 B C

ATOM 4182CB ALAB 27018.725-11.291-0.1071.00 46.74 B C

ATOM 4183C ALAB 27018.087-9.294 -1.4791.00 46.43 B C

ATOM 4184O ALAB 27019.077-9.094 -2.1871.00 46.56 B O

ATOM 4185N THRB 27116.845-9.053 -1.8891.00 45.32 B N

ATOM 4186CA THRB 27116.593-8.537 -3.2211.00 45.01 B C

ATOM 4187CB THRB 27115.206-8.958 -3.7291.00 45.38 B C

ATOM 4188OG1THRB 27114.19fi-8.508 -2.8211.00 46.37 B O

ATOM 4189CGZTHRB 27115.134-10.463-3.8451.00 45.74 B C

ATOM 4190C THRB 27116.725-7.022 -3.2531.00 44.93 B C

ATOM 4191O THRB 27116.826-6.420 -4.3211.00 45.10 B O

ATOM 4192N ASPB 27216.735-6.405 -2.0781.00 45.31 B N

ATOM 4193CA ASPB 27216.890-4.959 -2.0061.00 46.25 B C

ATOM 4194CB ASPB 27216.782-4.456 -0.5551.00 44.89 B C

ATOM 4195CG ASPB 27217.025-2.955 -0.4401.00 45.52 B C

ATOM 4196OD1ASPB 27216.710-2.238 -1.4081.00 47.47 B O

ATOM 4197OD2ASPB 27217.515-2.481 0.607 1.00 43.61 B O

ATOM 4198C ASPB 27218.274-4.651 -2.5711.00 46.57 B C

ATOM 4199O ASPB 27219.285-5.134 -2.0601.00 46.94 B O

ATOM 4200N METB 27318.314-3.850 -3.6271.00 47.22 B N

ATOM 4201CA METB 27319.573-3.497 -4.2681.00 48.41 B C

ATOM 4202CB METB 27319.334-2.519 -5.4181.00 48.65 B C

ATOM 4203CG METB 27318.793-3.174 -6.6711.00 49.34 B C

ATOM 4204SD METB 27319.868-4.504 -7.2391.00 51.75 B S

ATOM 4205CE METB 27321.413-3.630 -7.4341.00 49.57 B C

ATOM 4206C METB 27320.655-2.936 -3.3651.00 48.71 B C

ATOM 4207O METB 27321.833-3.162 -3.6201.00 50.14 B O

ATOM 4208N SERB 27420.284-2.209 -2.3181.0D 49.13 B N

ATOM 4209CA SERB 27421.307-1.642 -1.4431.00 49.79 B C

ATOM 4210CB SERB 27420.683-0.669 -0.4361.00 49.77 B C

ATOM 4211OG SERB 27419.882-1.350 0.511 1.00 49.44 B O

ATOM 4212C SERB 27422.078-2.741 -0.7051.00 _ B C
50.27 ATOM 4213O SERB 27423.091-2.472 -0.0611.00 49.88 B O

ATOM 4214N LYSB 27521.591-3.977 -0.8111.00 51.1 B N

ATOM 4215CA LYSB 27522.231-5.133 -0.1751.00 _ B C
51.84 ATOM 4216CB LYSB 27521.168-6.087 0.382 1.00 52.22 B C

ATOM 4217CG LYSB 27520.368-5.538 1.552 1.00 53.46 B C

ATOM 4218CD LYSB 27521.257-5.302 2.763 1.00 53.58 B C

ATOM 4219CE LYSB 27520.445-4.925 3.997 1.00 54 B C
.6 ATOM 4220NZ LYSB 27521.308-4.803 5.218 1.00 _ B N
_ 54.52 ATOM 4221C LYSB 27523.106-5.901 -1.1731.00 52.28 B C

ATOM 4222O LYSB 275_23_.893-6.766 -0.7871.00 51.20 B O

ATOM 4223N HISB 276_22.950-5.572 -2.4541.00 52.47 B N

ATOM 4224CA HISB 27623.680-6.211 -3.5471.00 53.24 B C

ATOM 4225CB HISB 27623.427-5.452 -4.846__ 52.28 B C
1.00 ATOM 4226CG HISB 27624.256-5.935 -5.992_ 51.23 B C
1.00 ATOM 4227CD2HISB 27625.364-5.415 -6.5691.00 49.98 B C

ATOM 4228ND1HISB 27623.987-7.108 -6.6641.00 50.69 B N
I

ATOM 4229CE1HISB 27624.892-7.288 -7.6081.00 49.91 B C

ATOM 4230NE2HISB 27625.739-6.274 -7.5721.00 49.31 B N

ATOM 4231C HISB 27625.193-6.376 -3.3671.00 54.42 B C

ATOM 4232O HISB 27625.7_09-7.494 -3.4271.0D 54.77 B O

ATOM 4233N METB 27725.905-5.270 -3.1751.00 55.05 B N

ATOM 4234CA METB 277_27._348-5.335 -3.0101.00 56.73 B C

ATOM 4235CB METB 27727.890-3.987 -2.5311.00 57.91 B C

ATOM 4236CG METB 27728.035-2.954 -3.6461.00 60.87 B C

ATOM 4237SD METB 27729.052-3.546 -5.0541.00 64.08 B S

ATOM 4238CE METB 27727.891-3.415 -6.4211.00 62.98 B C

ATOM 4239C METB 27727.809-6.449 -2 1.00 57.61 B C
.071 ATOM 42400 METB 27728.569-7.330 _ 1.00 57.88 B O
-2.479 ATOM 4241N ASNB 27827.346-6.425 -0.8241.00 58.15 B N

ATOM 4242CA ASNB 27827.740-7.447 0.140 1.00 58.19 B C

ATOM 4243CB ASNB 27827.158-7.132 1.523 1.00 58.97 B C

ATOM 4244CG ASNB 27827.733-5.851 2.122 1.00 59.74 B C

ATOM 4245ODtASNB 27828.892-5.495 1.875 1.00 59.00 B O

ATOM 4246ND2ASNB 27826.928-5.162 2.929 1.00 59.98 B N

ATOM 4247C ASNB 27827.366-8.871 -0.2741.00 57.88 B C

ATOM 4248O ASNB 27828.183-9.785 -0.1651.00 58.50 B O

ATOM 4249N LEUB 27926.141 -9.066-0.7481.00 57.27 B N

ATOM 4250CA LEUI 27925.706 -10.392-1.1751.00 57.15 B C
B

ATOM 4251CB LEUB 27924.290 -10.330-1.7481.00 56:64 B C
ATOM 4252CG LEUB 27923.114 -10.567-0.8061.00 56.83 B C

ATOM 4253CD1LEUB 27921.817 -10.486-1.5991.00 56.06 B C

ATOM 4254CD2LEUB 27923.241 -11.933-0.1451.00 57.00 B C

ATOM 4255C LEUB 27926.641 -10.982-2.2321.00 57.29 B C

ATOM 4256O LEUB 27926.855 -12.193-2.2821.00 56.52 B O

ATOM 4257N LEUB 28027.179 -10.115-3.0831.00 57.76 B N

ATOM 4258CA LEUB 28028.088 -10.525-4.1451.00 57.94 B C

ATOM 4259CB LEUB 28028.194 -9.413-5.1911.00 57.85 B C

ATOM 4260CG LEUB 28029.099 -9.606-6.4231.00 57.97 B C

ATOM 4261CD1LEUB 28028.685 -10.857-7.1861.00 57.88 B C

ATOM 4262CD2LEUB 28028.999 -8.383-7.3301.00 58.37 B C

ATOM 4263C LEUB 28029.470 -10.838-3.5721.00 58.33 B C

ATOM 4264O LEUB 28030.078 -11.852-3.9201.00 57.41 B O

ATOM 4265N ALAB 28129.962 -9.964-2.6981.00 58.82 B N

ATOM 4266CA ALAB 28131.268 -10.160-2.0851.00 60.12 B C

ATOM 4267CB ALAB 28131.595 -9.003-1.1551.00 59.19 B C

ATOM 4268C ALAB 28131.295 -11.476-1.3161.00 61.23 B C

ATOM 4269O ALAB 28132.290 -12.197-1.3521.00 61.84 B O

ATOM 4270N ASPB 28230.200 -11.786-0.6251.00 62.18 B N

ATOM 4271CA ASPB 28230.112 -13.0250.144 1.00 63.17 B C

ATOM 4272CB ASPB 28228.937 -12.9881.132 1.00 63.85 B C

ATOM 4273CG ASPB 28229.156 -12.0092.271 1.00 64.00 B C

ATOM 4274ODtASPB 28230.282 -11.9442.804 1.00 64.46 B O

ATOM 4275OD2ASPB 28228.193 -11.3122.647 1.00 65.43 B 0 ATOM 4276C ASPB 28229.949 -14.230-0.7691.00 63.30 B C

ATOM 4277O ASPB 28230.486 -15.300-0.4921.00 63.62 B O

ATOM 4278N LEU8 28329.199 -14.060-1.8531.00 63.83 B N

ATOM 4279CA LEUB 28328.992 -15.153-2..7961.00 64.40 B C

ATOM 4280CB LEUB 28327.966 -14.767-3.8681.00 64.03 B C

ATOM 4281CG LEUB 28327.780 -15.785-5.0001.00 63.55 B C

ATOM 4282CD1LEUB 28327.326 -17.108-4.4081.00 64.52 B C

ATOM 4283CD2LEUB 28326.767 -15.280-6.0171.00 63.09 B C

ATOM 4284C LEUB 28330.318 -15.500-3.4621.00 65.33 B C

ATOM 4285O LEUB 28330.600 -16.670-3.7261.00 64.72 B O

ATOM 4286N LYS8 28431.129 -14.480-3.7311.00 66.39 B N

ATOM 4287CA LYSB 28432.425 -14.692-4.3601.00 67.77 B C

ATOM 4288CB LYSB 28432.996 -13.367-4.8811.00 68.16 B C

ATOM 4289CG LYS8 28432.322 -12.890-6.1641.00 69.14 B C

ATOM 4290CD LYSB 28433.043 -11.711-6.7991.00 69.61 B C

ATOM 4291CE LYSB 28432.416 -11.374-8.1431.00 69.96 B C

ATOM 4292NZ LYSB 28433.139 -10.300-8.8681.00 70.33 B N

ATOM 4293C LYSB 28433.386 -15.331-3.3701.00 68.27 B C

ATOM 4294O LYSB 28434.083 -16,293-3.6981.00 67.89 B O

ATOM 4295N THRB 28533.410 -14.796-2.1561.00 69.10 B N

ATOM 4296CA THRB 28534.272 -15.326-1.1181.00 70.30 B C

ATOM 4297CB THRB 28534.085 -14.5600.202 1.00 70.19 B C

ATOM 4298OG1THRB 28534.649 -13.2470.072 1.00 70.40 B O

ATOM 4299CG2THRB 28534.772 -15.2881.346 1.00 70.57 B C

ATOM 4300C THRB 28533.962 -16.799-0.8961.00 71.23 B C

ATOM 4301O THRB 28534.858 -17.586-0:6061.00 71.50 B O

ATOM 4302N METB 28632.697 -17.177-1.0471.00 72.30 B N

ATOM 4303CA METB 28632.311 -18.569-0.8531.00 73.68 B C

ATOM 4304CB METB 28630.806 -18.698-0.5941.00 73.80 B C

ATOM 4305CG METB 28630.422 -20.077-0.0731.00 75.15 B C

ATOM 4306SD METB 28628.659 -20.3950.100 1.00 76.29 B S

ATOM 4307CE METB 28628.340 -21.221-1.4591.00 75.00 B C

ATOM 4308C METB 28632.695 -19.441-2.0451.00 _ B C
74.32 ATOM 4309O METB 28632.876 -20.647-1.9001.00 74.51 B O

ATOM 4310N VALB 28732.806 -18.835-3.2241,00 75.21 B N

ATOM 4311CA VALB 28733.183 -19.573-4.4241.00 75.80 B C

ATOM 4312CB VALB 28732.824 -18.781-5.7191.00 75.44 B C

ATOM 4313CG1VALB 28733.447 -19.444-6.9421.00 74.84 B C

ATOM 4314CG2VALB 28731.310 -18.727-5.8901.00 74:40 B C

ATOM 4315C VALB 28734.686 -19.825-4.3621.00 76.79 B C

ATOM 4316O VALB 287_35.189-20.791-4.9401.00 76.87 B O

ATOM 4317N GLUB 28835.389 -18.957-3.6371.00 77.68 B N

ATOM 4318CA GLUB 28836.838 -19.067-3.4681.00 78.87 B C

ATOM 4319CB GLUB 28837.410 -17.783-2.8571.00 79.98 B C

ATOM 4320CG GLUB 28837.199 -16.517-3.6791.00 82.17 B C
~

ATOM 4321CD GLUB 28837.763 -15.277-2.9921.00 83.77 B C

ATOM 4322OE1GLUB 28838.998 -15.220-2.7821.00 83.95 B O

ATOM 4323OE2GLUB .25836.972 -14.362-2.6581.00 84.16 B O

ATOM 4324C GLUB 28837.178 -20.235-2.5481.00 78.74 B C

ATOM 4325O GLUB 28838.194 -20.908- 1.00 79.17 B O
2.726 ATOM 4326N THRB 28936.322 -20.462_ 1.00 78.25 B N
-1.558 ATOM 4327CA THRB 28936.523 -21.533-0.5961.00 77.62 B C

ATOM 4328CB THRB 28936.370 -20.9940.839 1.00 77.49 B C

ATOM 4329OG1THRB 28935.017 -20.5721.058 1.00 76.42 B O

ATOM 4330CG2THRB 28937.295 -19.8041.049 1.00 77.09 B C

ATOM 4331C THRB 28935.528 -22.672__ 1.00 77.73 B C
-0.8 ATOM 4332O THRB 28935.277 -23.476_ 1.00 77.93 B O
0.076 ATOM 4333N LYSB 29034.974 -22.731-2.0291.00 77.97 B N

ATOM 4334CA LYSB 29033.995 -23 -2 1 00 78 B C
I I I I I ~ ~ 749 421 37 ATOM 4335CB LYSB 29033.805-23.7093.945 1.00 78.22 B C

ATOM 4336CG LYSB 29032.752-24.658-4.5031.00 77.87 B C

ATOM 4337CD LYSB 29032.759-24.623-6.0291.00 77.78 B C

ATOM 4338CE LYSB 29031.809-25.652-6.6211.00 78.26 B C

ATOM 4339NZ LYSB 29031.883-25.705-8.1111.00 78.10 B N

ATOM 4340C LYSB 29034.389-25.165-1.9791.00 78.73 B C

ATOM 4341O LYSB 29035.572-25.512-1.9531.00 78. B O

ATOM 4342N LYSB 29133.389-25.973-1.6301.00 _ B N
79.03 ATOM 4343CA LYSB 29133.617-27.345-1.1911.00 79.20 B C

ATOM 4344CB LYS. 29133.505-27.3900.329 1.00 80.06 B C
B

ATOM 4345CG LYSB 29135.077-26.7040.797 1.00 81.24 B C

ATOM 4346CD LYSB 29135.211-26.7182.302 1.00 82.48 B C

ATOM 4347CE LYSB 29136.479-25.9922.723 1.00 83.56 B C

ATOM 4348NZ LYSB 29136.628-25.9254.205 1.00 84.41 B N

ATOM 4349C LYSB 29132.485-28.275-1.5961.00 78.93 B C

ATOM 43500 LYSB 29131.311-27.909-1.5371.00 78.50 B O

ATOM 4351N VALB 29232.852-29.486-2.0021.00 79.16 B N

ATOM 4352CA VALB 29231.882-30.487-2.4281.00 79.71 B C

ATOM 4353CB VALB 29231.953-30.713-3.9541.00 79.54 B C

ATOM 4354CG1VACB 29231.592-29.437-4.6901,00 79.32 B C

ATOM 4355CG2VALB 29233.352-31.171-4.3431.00 79.45 B C

ATOM 4356C VALB 29232.12031.830 -1.7501.00 80.13 B C

ATOM 4357O VALB 29233.089-32.007-1.0131.00 80.28 B O

ATOM 4358N THRB 29331.225-32.773-2.0111.00 80.99 B N

ATOM 4359CA THRB 29331.336-34.114-1.4551.00 82.11 B C

ATOM 4360CB THRB 29329.944-34.735-1.1761.00 81.87 B C

ATOM 4361OG1THRB 29329.272-34.989-2.4171.00 82.04 B O

ATOM 4362CG2THRB 29329.098X3.794 -0.3401.00 81.73 B C

ATOM 4363C THRB 29332.058-34.974-2.4901.00 82.97 B C

ATOM 4364O THRB 29332.656-34.453-3.4321.00 82.97 B O

ATOM 4365N SERB 29431.998-36.290-2.3261.00 84.10 B N

ATOM 4366CA SERB 29432.664-37.186-3.2651.00 85.38 B C

ATOM 4367CB SERB 29432.710-38.607-2.6991.00 85.80 B C

ATOM 4368OG SERB 29433.365-35.623-1.4431.00 87.18 B 0 ATOM 4369C SERB 29431.959-37.199-4.6161.00 85.68 B C

ATOM 4370O SERB 29432.613-37.204-5.6641.00 85.11 B O

ATOM 4371N SERB 29530.62637.201 -4.5861.00 85.94 B N

ATOM 4372CA SERB 29529.83537.218 -5.8131.00 55.91 B C

ATOM 4373CB SERB 29528.379-37.600-5.5061.00 85.75 B C

ATOM 4374OG SERB 29527.809-36.765-4.5151.00 85.70 B 0 ATOM 4375C SERB 29529.886X5.881 -6.5551.00 85.73 B C

ATOM 4376O SERB 29529.43735.771 -7.7041.00 86.11 B O

ATOM 4377N GLYB 29630.456-34.873-5.9001.00 84.63 B N

ATOM 4378CA GLYB 29630.560-33.561-6.5071.00 83.05 B C

ATOM 4379C GLYB 29629.390-32.670-6.1491.00 82.07 B C

ATOM 4380O GLYB 29629.201-31.619-6.7581.00 82.15 B O

ATOM 4381N VALB 29728.595-33.0945.171 1.0D 81.18 B N

ATOM 4382CA VALB 29727.447-32.307-4.7361.00 _ B C
80.4 ATOM 4383CB VALB 29726.465-33.153-3.8941.00 _ B C
80.54 ATOM 4384CG1VAL8 29725.274-32.303-3.4771.00 __ B C
80.28 ATOM 4385CG2VALB 29725.999-34.363-4.6951.00 80.32 B C

ATOM 4386C VALB 29727.974-31.162-3.8821.00 79.60 B C

ATOM 4387O VALB 297_28.788-31.382-2.9851.00 79.42 B O

ATOM 4388N LEUB 29827.521-29.944-4.1641.00 78.84 B N

ATOM 4389CA LEUB 29827.970-28.774-3.4081.00 78.37 B C

ATOM 4390CB LEUB 29827.217-27.525-3.8641.00 78.36 B C

ATOM 4391CG LEUB 29828.019-26.221-3.8801.00 78.29 B C

ATOM 4392CD1LEUB 29827.059. -25.061-4.1031.00 78.79 B C

ATOM 4393CD2LEUB 29828.780-26.039-2.5801.00 78.68 B C

ATOM 4394C LEUB 29827.751-28.982-1.9081.00 77.95 B C

ATOM 4395O LEUB 29826._653-29.340-1.4741.00 77.10 B O

ATOM 4396N LEUB 29928.796-28.742-1.1201.00 77.51 B N

ATOM 4397CA LEUB 29928.713-28.9300.325 1.00 77.23 B C

ATOM 4398CB LEUB 29930.015-29.5540.846 1.00 77.62 B C

ATOM 4399CG LEUB 29930.03230.228 2.226 1.00 78.06 B C

ATOM 4400CD1LEUB 2992_9.842-29.2013.334 1.00 78.02 B C

ATOM 4401CD2LEUB 29928.943-31.2952.280 1.00 78,08 B C

ATOM 4402C LEUB 29928.427-27.6331.070 1.00 76.56 B C

ATOM 4403O LEUB 29929.332-26.8361.317 1.00 76.30 B O

ATOM 4404N LEUB 30027.161-27.4331.426 1.00 76.07 B N

ATOM 4405CA LEUB 30026.740-26.2472.163 1.00 75.56 B C

ATOM 4406CB LEUB 30025.450-25.6841.568 1,00 75.29 B C

ATOM 4407CG LEUB 30025.600-25.2130. 1.00 75.26 B C

ATOM 4408CD1LEUB 30024.262-24.702_ 1.00 75.52 B C
-0.409 ATOM 4409CD2LEUB 30026.662-24.1260.040 1.00 73.88 B C

ATOM 4410C LEUB 30026.540-26.6343.623 1.00 75.52 B C

ATOM 4411O LEUB 30025.481-27.121__ 1.00 74.85 B O
4.026 ATOM 4412N ASPB 30127.590-26.4074. 1.00 75.32 B N

ATOM 4413CA ASPB 30127.633-26.732_ 1.00 75.71 B C
5.819 ATOM 4414CB ASPB 30129.016-26.3606.360 1.00 76.99 B C

ATOM 4415CG ASPB 30129.200-26.7517.804 1.00 77.78 B C

ATOM 4416OD1ASPB 30130.095-26.1758.460 1.00 78.63 B O

ATOM 4417OD2ASPB 30128.460-27.6408.277 1.00 78.65 B O

ATOM 4418C ASPB 30126.561-26.0856.702 1.00 75.26 B C

ATOM 44190 ASP8 30125.494-26.6596.934 1.00 75.62 B 0 ATOM 4420N ASNB 30226.877-24.8897.195 1.00 74.02 B N

ATOM 4421CA ASNB 30226.017-24.1208.090 1.00 72,29 B
ATOM 4422CB ASNB 30226.895-23.1658.891 1.00 72.79 B C
ATOM 4423CG ASNB 30227.690-22.235_ 8.0011.00 72,95 B C
ATOM 4424ODtASNB 30227.132-21.3367.377 1.00 73.33 B O
ATOM 4425ND2ASNB 30228.998-22.4547.926 1.00 72.86 B N
ATOM 4426C ASNB 30224.890-23.3337.413 1.00 70.95 B C
ATOM 44270 ASNB 30224.803-23.2796.187 1.00 71,27 B O
ATOM 442$N TYRB 30324.035-22.7158.227 1.00 69.08 B N
ATOM 4429CA TYRB 30322.907-21.9367.720 1.00 66.70 B C
ATOM 4430CB TYRB 30322.003-21.4918.870 1.00 66.17 B C
ATOM 4431CG TYRB 30320.733-20.8058.409 1.00 66,06 B C
ATOM 4432CDtTYRB 30319.675-21.5427.879 1.00 65.39 B C
ATOM 4433CE1TYRB 30318.517-20.9167.429 1.00 65.68 B C
ATOM 4434CD2TYRB 30320.600-19.414$.479 1.00 65.28 B C
ATOM 4435CE2TYRB 30319.445-18.7778.031 1.00 65.07 B C
ATOM 4436CZ TYRB 30318.408-19.5337.507 1.00 65.83 B C
ATOM 4437OH TYRB 30317.266-18.9147.049 1.00 66.54 B O
ATOM 4438C TYRB 30323.383-20.7076.958 1.00 65.49 B C
ATOM 4439O TYRB 30322.840-20.3655.911 1.00 65.03 B O
ATOM 4440N SER8 30424.392-20.0367.496 1.00 64.44 B N
ATOM 4441CA SERB 30424.936-18.8556.847 1.00 63.70 B C
ATOM 4442C8 SERB 30426.261-18.4617.501 1.00 63.77 B C
ATOM 4443OG SERB 3D426.918-17,4446.764 1.00 65.15 B O
ATOM 4444C SERB 3D425.151-19.1445.364 1,00 63.36 B C
ATOM 4445O SERB 30424.658-18.4134.504 1.00 $4,17 B O
ATOM 4446N ASPB 30525.873-20.2245.075 1.00 61.99 B N
ATOM 4447CA ASPB 30526.167-20.6223.703 1.00 60.99 B C
ATOM 4448CB ASPB 30527.136-21.8073.684 1.00 61.70 B C

. -21.4724.278 1.00 62.44 B C
ATOM 4450OD1ASPB 3058 -20.4763.838 1.00 63.50 B O
ATOM 4451002ASPB 30529.089-22.2085.180 1.00 63.56 B O
ATOM 4452C ASPB 30528.940-21.0082.897 1.00 59.75 B C
ATOM 4453O ASPB 30524.934-20.5111.795 1,00 59.51 B O
ATOM 4454N ARGB 30624.731 . -21.9053.451 1.00 58.52 B N
ATOM 4455CA ARGB 3064 -22.3942.780 1.00 57.75 B C
ATOM 4456CB ARGB 30622.922-23.3883.684 1.00 56.99 B C
ATOM 4457CG ARGB 30622.179-24.5644.154 1.00 56.58 B C
ATOM 4458CD ARGB 30623.028-25.5015.084 1.00 56.16 B C
ATOM 4459NE ARGB 30622.257-26.3514,372 1.00 55.75 B N
ATOM 4460C2 ARGB 30621.303-27.2323.435 1.00 56.01 B C
ATOM 4461NH1ARGB 30621.644-27.3813.092 1.00 56,28 B N
ATOM 4462NH2ARGg 30622.919 . -27.9652.839 1.00 54.54 B N
ATOM 4463C ARGB 3064 -21.2942.345 1.00 58.03 g C
ATOM 4464O ARGB 30621.956-21.3471.240 1.00 57.94 B O
ATOM 4465N ILEB 30721.407-20.3063.213 1.00 57.67 B N
ATOM 4466CA ILEB 30721.742 . -19.2102,909 1.00 56.69 B C
ATOM 4467CB ILEB 30720.367-18.4824.201 1.00 55.87 B C
ATOM 4468CG2iLEB 30727.534-17.7124.814 1.00 54.64 B C
ATOM 4469CG1ILEB 30719.200-17.5453.882 1.00 54.52 B C
ATOM 4470CD1ILEg 30717.947-18.2673.435 1.00 53.62 B C
ATOM 4471C tLEB 30721.457-18.1951.962 1.00 56.41 B C
ATOM 4472O ILE8 30720.788-17.6341.100 l,pp x_48 g O
ATOM 4473N GLNB 3D822.754-17.9712.128 1.00 57.02 B N
ATOM 4474CA GLNB 30823.493-17.0371.291 1.00 57.71 B C
ATOM 4475CB GLNB 30824.935-16.9851.778 1.00 59.66 B C
ATOM 4476CG GLNB 30825.799-15.9271.154 1.00 62.88 g C
ATOM 4477CD GLNB 30827.156-15.8521.829 1.00 65.66 B C
ATOM 4478OE1GLNB 30827.253-15.5503.027 1,00 66.37 B O
ATOM 4479NE2GLNB 30828.216-16.1381,069 1.00 66.16 B N
ATOM 4480C GLNB 30823.422-17.488-0.1751.00 57.33 B C
ATOM 4481O GLNB 30$23.497-16.675-1.0971.00 57.80 B O
ATOM 4482N VALB 30923.265-18.791-0.3831.00 56.08 B N
ATOM 4483CA VALB 30923.161-19.347-1,7281.00 54.83 B C
ATOM 4484CB VALB 30923.516-20.864-1.7461.00 55.06 B C
ATOM 4485CG1VALB 30923.266-21.454-3.1281,00 55.21 B C
ATOM 4486CG2VALB 30924.970-21.059-1,3611.00 54.97 B C
ATOM 4487C VAL8 30921.736-19.160-2.2451,00 53.73 B C
ATOM 4488O VALB 30921.527-18.893-3.4281.00 53.52 B O
ATOM 4489N LEUB 31020.753-19.310-1.3601.00 52.45 B N
ATOM 4490GA LEUB 31019.358-19.134-1,7581.00 51.33 B C

. -19.646-0.6651.p0 50.75 B C
ATOM 4492CG LEUB 31018.395-21,166-0.4791,00 50.71 B C
ATOM 4493CD1LEUB 31017.430-21.5360.630 1,00 50.97 8 C
ATOM 4494CD2LEUB 31017.989-21.848-1.7781.00 49.98 B C
ATOM 4495C LEUB 31019.114-17.650-2.0321.00 49.86 B C
ATOM 4496O LEU-B 31018,447-17,290-2.9991,0p 49.43 B O
ATOM 4497N GLNB 31118.678-16.798-1.1811.00 48.40 B N
ATOM 4498CA GLNB 31119.549-15.360-1,3431,00 47.54 B C

. -14.626-0.2581.00 45.17 B C
ATOM 4500CG GLN8 31119,752-14.7711.131 1,00 43.47 B C
ATOM 4501CD GLNB 31120.570-14.0502.186 1.00 44.30 B C
ATOM 4502OE1GW B 31121.796-14.9762.223 1.00 44.55 B O
ATOM 4503NE2GLNB 31119.895-13.2983.059 1.00 42.43 B N
ATOM 4504C GLNB 31720.054-14.957-2,7291.00 47.92 B C
ATOM 4505O GLNB 31119.289-14.432-3.5431.00 48.67 B O
ATOM 4506N ASNB 31221.332-15.211-3.0061,00 47.21 g N

ATOM 4507CA ASNB 31221.896-14.859-4.3121.00 46.27 B C

ATOM 4508__CB ASNB 31223.358-15.190-4.3551.00 45.42 B C

ATOM 4509CG ASNB 31224.230-14.148_ -3.6361.00 45.46 B C

ATOM 4510OD1ASNB 3i224.407-13.030-4.1271.00 45.63 B O

ATOM 4511ND2ASNB 31224.740-14.502-2.4611.00 44.96 B N

ATOM 4512C ASNB 31221.163-15.545-5.4661.00 45.70 B C

ATOM 4513O ASNB 31221.027-14.969-6.5531.00 43.94 B 0 ATOM 4514N METB 31320.671-16.761-5.2301.00 45.40 B N

ATOM 4515CA METB 31319.948-17.475-6.2771.00 45.95 B C

ATOM 4516CB METB 31319.528-18.876-5.8191.00 46.60 B C

ATOM 4517CG METB 31318.990-19.747-6.9601.00 47.46 B C

ATOM 4518SD METB 31318.145-21.261-6.4221.00 49.90 B S

ATOM 4519CE METB 31319.501-22.076-5.5641.00 50.22 B C

ATOM 4520C METB 31318.703-16.679-6.6771.00 45.18 B C

ATOM 4521O METB 31318.507-16.367-7.8571.00 43.85 B O

ATOM 4522N VALB 31417.867-16.347-5.6971.00 44.68 B N

ATOM 4523CA VALB 31416.661-15.583-5.9851.00 44.78 B C

ATOM 4524CB VALB 31415.765-15.451-4.7371.00 45.13 B C

ATOM 4525CGtVALB 31414.569-14.557-5.0421.00 45.05 B C

ATOM 4526CG2VALB 31415.273-16.828-4.3181.00 44.51 B C

ATOM 4527C VALB 31417.037-14.201-6.5161.00 44.41 B C

ATOM 45280 VALB 31416.313-13.619-7_3271.00 44.73 B 0 ATOM 4529N HISB 31518.182-13.687-6.0731.00 43.41 B N

ATOM 4530CA HISB 31518.659-12.384-6.5301.00 43.22 B C

ATOM 4531CB HISB 31519.880-11.959-5.7021.00 41.68 B C

ATOM 4532CG HISB 31520.426-10.609-6.0551.00 41.03 B C

ATOM 4533__CD2HISB 31521.697-10.140-6.0651.00 39.70 B C

ATOM 4534ND1HISB 31519.621-9.534 -6.3711.00 41.55 B N

ATOM 4535CE1HISB 31520.373-8.463 -6.5591.00 39.85 B C

ATOM 4536NE2HISB 31521.636-8.804 -6.3791.00 39.29 B N

ATOM 4537C HISB 31519.005-12.453-8.0211.00 44.21 B C

ATOM 4538O HISB 31518.710-11.568-8.8001.00 45.49 B 0 ATOM 4539N CYSB 31619.621-13.596-8.4191.00 43.69 B N

ATOM 4540CA CYSB 31619.965-13.803-9.8211.00 43.02 B C

ATOM 4541CB CYSB 31620.812-15.078-9.9951.00 42.99 B C

ATOM 4542SG CYSB 31622.557-14.927-9.4671.00 43.93 B S

ATOM 4543C CYSB 31618.686-13.908-10.6541.00 42.85 B C

ATOM 4544O CYSB 31618.613-13.368-11.7581.00 42.85 B O

ATOM 4545N ALAB 31717.680-14.600-10.1251.00 42.79 B N

ATOM 4546CA ALAB 31716.407-14.752-10.8361.00 43.95 B C

ATOM 4547CB ALAB 31715.464-15.655-10.0421.00 43.84 B C

ATOM 4548C ALAB 31715.755-13.383-11.0571.00 44.14 B C

ATOM 4549O ALAB 31715.312-13.056-12.1631.00 43.44 B O

ATOM 4550N ASPB 31815.702-12.591-9.9891.00 45.04 B N

ATOM 4551CA ASPB 31815.123-11.254-10.0451.00 45.37 B C

ATOM 4552CB ASPB 31815.158-10.617-8.6421.00 45.90 B C

ATOM 4553CG ASPB 31814.351-9.324 -8.5461.00 45.02 B C

ATOM 4554OD2ASPB 31814.879-8.354 -7.9701.00 46.42 B O

ATOM 4555C ASPB _31815.911-10.418-11.0591.00 45.19 B C
_ ATOM 4556O ASPB 31815.330-9.622 -11.7931.00 45.10 B 0 ATOM 4557OD1ASPB 31813.1_91-9.271 -9.0201.00 46.73 B 0 ATOM 4558N LEUB 31917.226-10.616-11.1181.00 45.21 B N

ATOM 4559CA LEUB 31918.057-9.878 -12.0651.00 45.75 B C

ATOM 4560CB LEUB 31919.320-9.371 -11.3711.00 45.23 B C

ATOM 4561CG LEUB 31919.089-8.299 -10.3141.00 46.07 B C

ATOM 4562CD1LEUB 31920.414-7.687 -9.8921.00 46.43 B C

ATOM 4563CD2LEUB 31918.187-7.231 -10.8911.00 47.16 B C

ATOM 4564C LEUB 31918.440-10.760-13 1.00 46.59 B C

ATOM 4565O LEUB 31919.587-10.746_ 1.00 46.68 B O
-13.704 ATOM 4566N SERB 32017.469-11.503-13.7751.00 47.30 B N

ATOM 4567CA SERB 32017.726-12.423-14.8781.00 47.54 B C

ATOM 4568CB SERB 32017.067-13.769-14.5861.00 47.46 B C

ATOM 4569OG SERB 32015.670-13,706-14.8331.00 47.75 B O

ATOM 4570C SERB 32017.299-11.992-16.2721.00 48.60 B C

ATOM 4571O SERB 32017.742-12.588_ 1.00 50.89 8 O
-17.251 ATOM 4572N ASNB 32116.437-10.989-16.3951.00 48.13 B N

ATOM 4573CA ASNB 32116._006-10.589-17.7281.00 47.80 B C

ATOM 4574CB ASNB 32114.934-9.473 -17.6501.00 48.79 B C

ATOM 4575CG ASNB 32115.425-8.212 -16.9691.00 49.51 B C

ATOM 4576OD1ASNB 32116.015-7.335 -17.6031.00 49.54 B 0 ATOM 4577ND2ASNB 32115.184-8.114 - 1.00 50.45 B N
15.666 ATOM 4578C ASNB 32117.144-10.221_ 1.00 46.31 B C
-18.706 ATOM 45790 ASNB 32117.016-10.425-19.9111.00 45.64 B 0 ATOM 4580N PROB 32218.275-9.692 -18. 1.00 45.07 B N

ATOM 4581CD PROB 322-18.586-9.026 _ 1.00 44.74 B C
_ .937 ATOM 4582CA PROB 32219.296-9.383 _ 1.00 45.53 B C
--19.219 ATOM 4583CB PROB 32220.277-8.488 -18.4601.00 43.83 B C

ATOM 4584CG PROB 32219.425-7.857 -17.3991.00 43.46 B C

ATOM 4585C PROB 32219.974-10.648-19.7691.00 46.83 B C

ATOM 4586O PROB 32220.683-10.591-20.7711.00 46.28 B O

ATOM 4587N THRB 32319.745-11.785-19.1111.00 48.66 B N

ATOM 4588CA THRB 32320.347-13.058-19.5161.00 49.77 B C

ATOM 4589CB THRB 32320.833-13.582-18.3111.00 49.25 B C

ATOM 4590OG1THRB 32319.707-14.533-17.7051.00 47.83 B O

ATOM 4591CG2THRB 32321.542-12.992-17.2911.00 47.65 B C

ATOM 4592C THRB 32319.388-13.963-20.2721.00 51.33 B C

ATOM4593 T HR B 23 19,712-15.11720.553 1.00 52.23 0 ATOMO N '~ 3 24 98.202-13.458-20.575 1.00 B N
ATOM4594 L YS B 24 17.219-14.242-21.307 1.00 52.06 C
ATOM4595 CA ' 3 324 15.809-13.878-20.841 1.00 B B C
ATOM4596 L YS B 324 15.516-14.188-19.387 1.00 52.91B C
ATOM4597 CB 1 3 324 15.292-15.669-19.169 1.00 B B C
ATOM4598 CG LYSB 324 14.786-15.946-17.763 1.00 52.77B C
ATOM4599 CD ' B 324 13,472-15.283-17.517 1.00 53.59B N
4600 CE LYSB 939 800 1.00 55.30B C
NZ ' B 13 -22 56.21 ~ 53.71 LYS
LYS
' ATOM4601 C LYSB 324 17,355. . 1.00 54.09B 0 ATOM4602 O LYSB 324 17.936- -23.188 1.00 54.37B N
ATOM4603 N PROB 325 16.825-12.922-23.663 1.0D 53.71B C
ATOM4604 CD PROB 325 16.026-14.821-23.421 1.00 54.64B C
ATOM4605 CA PROB 325 16.943-16.036-25.097 1.00 54-08B C
ATOM4606 CB PROB 325 16.077-14.535-25:740 1.00 54.03B C
ATOM4607 CG PROB 325 15.141-15.624-24.622 1.00 55.72B C
ATOM4608 C PROB 325 16.475-16.066-25.422 1.00 55.438 O
-13.103915 ATOM4609 O PROB 325 15.446. . 1.00 55.998 N
ATOM4610 N LEUB 326 17.256- -26.250 1.00 57.03B C
-12.411652 ATOM4611 CA LEUB 326 16.982-11.43. 1.00 56.96B C
ATOM4612 CB LEUB 326 17.647-10.744-27.997 1.00 57.34B C
ATOM4613 CG LEUB 326 1T.692-9.290-28.462 1.00 57.82B C
ATOM4614 CD1LEUB 326 18.475-8.462-27.456 1.00 57.15B C
ATOM4615 CD2LEUB 326 18.340-9.215-29.838 1.00 57.20B C
ATOM4616 C LEUB 326 15.503-10.664-26.736 1.00 57.41B O
ATOM4617 O LEUB 326 15.065-9.886-26.128 1.00 57.63B N
ATOM4618 N GLNB 327 14.739-11:444-27.492 1.00 57.93B C
ATOM4619 CA GLNB 327 13.303-t -27.657 1.00 60.13B C
ATOM4620 CB GLNB 327 12.6551.204 -28.327 1.00 63'20B C
ATOM4621 CG GLNB 327 11.167-12.412-28.585 1.00 65.01B C
. 4622 CD GLNB 327 10.422-12.260-28.888 1.00 65.83B O
ATOM4623 OE7GLNB 327 10.132-13.565-27:252 1.00 65.35B N
ATOM4624 NE2GLNB 327 10.123-13.961-29.493 1.0D 56.44B C
ATOM 9 -14.254-26.332 ATOM4625 C GLNB 327 12.57 . -26.287 1.00 56.07B 0 ATOM4626 O GLNB 327 11.638-10.116268 1.00 54.73B N

ATOM N LEUB 328 13.008. . 1.00 53.53B C
4627 CA LEUB 328 12.423- -23.945 1.00 53.73B C
ATOM CB LEUB 328 12.732-11.413-23.048 1.00 55.06B C
4628 CG LEU8 328 11.936-12.619-23,229 1.00 54.19B C
ATOM CD1LEUB 328 12.479-13.915-22.281 1.0D 54-97B C
4629 CD2LEUB 328 10.451-14.991-22;957 1.00 52.46B C
ATOM C LEUB 328 12-994-13.652-23.301 1.00 52.18B O
4630 O LEUB 328 12.2fi5-10.155-22.997 1.00 50.52B N
ATOM N TYRB 329 14.308-9.211-23.099 1.00 48.52B C
4631 CA TYRB 329 15.022-10.162-22.496 1.00 44.67B C
ATOM CB TYRB 329 16.512-9.045-22.842 1.00 42.16B C
4632 -9.177284 ATOM

ATOM

ATOM

ATOM

ATOM CG TYRB 329 17.443. . 1.00 41.00B C
4638 CD11YRB 329 17.105- -21.159 1.00 38.3AB C
ATOM CE1TYRB 329 17.951-7.359-20.637 1.00 40.68B C
4639 CD2TYRB 329 18.690-6.409-22.865 1.00 39.00B C
ATOM CE2TYRB 329 19.580-7.902-22.347 1.00 38.008 C
4640 CZ TYRB 329 19.224-6.964-21.236 1.00 36.93B O
ATOM OH TYRB 329 20.103-6.217-20.753 1.00 49.49B C
4641 -5.267944 ATOM

ATOM

ATOM4645 C TYRB 329 14.468. . 1.00 50.23B O
ATOM4646 O TYRB 329 14.183- -22.107 1.00 49.938 N
ATOM4647 N ARG8 330 14.289-6.829-24.244 1.00 50.398 C
-7.495758 ATOM CA ARGB 330 13.786-6.21 . 1.00 50.89B C
4648 CB ARG8 330 13.808-6.214-26.295 1.00 52.06B C
ATOM CG ARGB 330 15.227-6.159-26.882 1.00 53.07B C

ATOM CD ARGB 330 15.219. . 1.00 54.16B N
4651 NE ARGB 330 14.669- -29.005 1.00 55.44B C
ATOM CZ ARG8 330 14.463-4.993-30.310 1.00 55.54B N
4652 NH1ARGB 330 14.760-4.828-31.163 1.00 55.03B N
ATOM NH2ARGB 330 13.969-5.806-30-76fi 1.00 49.81B C
4653 -3.681244 ATOM

ATOM C ARGB 330 12.397. . 1.00 49.30B 0 4656 O ARGB 330 12.157- -23.951 1.00 48.36B N
ATOM N GLNB 331 11.485-4.653-24.137 1.00 48.64B C
4657 CA GLNB 331 10.154-6.790-23.627 1.00 48.80B C
ATOM -6.485665 ATOM CB GLNB 331 9.259 . . 1.00 50.71B C
4664 CG GLNB 331 9.168 - -25.026 1.00 51.29B C
ATOM CD GLNB 331 8.159 x.365 -25.065 1.00 51.60B O
4661 OE1GLNB 331 6.950 -9.493-24.963 1.00 51.29B N
ATOM NE2GLNB 331 8.652 -9.265-25.207 1.00 48.54B C
4662 C GLNB 331 10-278-10.724-22.182 1.00 47.93B O
ATOM O GLNB 331 9.650 -5,993-21.801 1.00 47.23B N
4663 N TRPB 332 11.099-4.998-21.392 1.00 46.72B C
ATOM CA TRPB 332 11.325-6.691-19.992 1 15 B C
4664 -6.3281 00 45 ATOM

ATOM

ATOM

ATOM

ATOM CB TRPB 332 12.254-7.333-19.29 . . B C
4669 CG TRPB 332 11.626-8.654-18.975 1.00 44.69B C
ATOM 210 1 44.73 ATOM CD2TRPB 332 10.434-8.888. . 44.40B C
4671 CE2TRPB 332 10.225-10.285- 21.00 44.36B C
ATOM CE3TR P 3322 9.524 -8.054-18.18321.000 44.61B C
4672 CD1TR . 332 12.076-9.880-17.5421.00 44.90 N
ATOM NE1TR B 3322 11.2A3-10.863-19.3691.0 0 44.0B C
4673 CZ2TR P 33 9.139 -10.872-18.8961.0 0 42.91 B
ATOM CZ3TR B B fi.440-8.639-17.5131.0 0 43.9B C
4674 P 33 -16.87 1 9 B

ATOM B

ATOM

ATOM CH2TR P B 2 8.260 -10.035. .

ATOM 4679C TRPB 33211.940 -4.944-19.8831.00 45.92 B C

ATOM 4680O TRPB 33211.489 -4.120-19.0911.00 45.63 B O

ATOM 4681N THRB 33312.970 -4.687-20.6801.00 45.56 B N

ATOM 4682CA THRB 33313.626 -3.389-20_6331.00 46.66 B C

ATOM 4683CB THRB 33314.806 -3.328-21.6061.00 45.41 B C

ATOM 4684OG1THRB 33315.768 -4.317-21.2301.00 46.88 B 0 ATOM 4685CG2THRB 33315.464 -1.959-21.5601.00 43.68 B C

ATOM 4686C THRB 33312.658 -2.254-20.9451.00 47.18 B C

ATOM 46870 THRB 33312.691 -1.209-20.3011.00 48.31 B O

ATOM 4688N ASPB 33411.800 -2.455-21.9361.00 47.84 B N

ATOM 4689CA ASPB 33410.832 -1.426-22.2911.00 47.92 B C

ATOM 4690__CB ASPB 33410.042 -1.823-23.5431.00 48.06 B C

ATOM 4691CG ASPB 33410.911 -1.891-24.7731.00 49.03 B C

ATOM 4692OD1ASPB 33411.926 -1.165-24.8191.00 50.50 B 0 ATOM 4693OD2ASPB 33410.581 -2.657-25.6991.00 50.33 B O

ATOM 4694C ASPB 3349.874 -1.204-21.1291.0D 47.31 B C

ATOM 4695O ASPB 3349.563 -0.063-20.7861.00 47.64 B O

ATOM 4696N ARGB 3359.422 -2.301-20.5221.00 45.72 B N

ATOM 4697CA ARGB 3358.496 -2.229-19.4031.00 43.89 B C

ATOM 4698CB ARGB 3358.037 -3.630-19.0121,00 42.36 B C

ATOM 4699CG ARGB 3357.261 -4.330-20.0951.00 40.23 B C

ATOM 4700CD ARGB 3356.459 -5.460-19.5241.00 41.46 B C

ATOM 4701NE ARGB 3355.583 -6.047-20.5241.00 43.06 B N

ATOM 4702CZ ARGB 3354.369 -6.507-20.2591.00 43.73 B C
' ATOM 4703NH1ARGB 3353.897 -6.438-19.0191.00 43.84 B N

ATOM 4704NH2ARGB 3353.633 -7.042-21.2241.00 43.33 B N

ATOM 4705C ARGB 3359.066 -1.514-18.1731.00 44.11 B C

ATOM 4706O ARGB 3358.352 -0.760-17.4981.00 44.18 B O

ATOM 4707N ILEB 33610.342 -1.738-17.8771.00 42.18 B N

ATOM 4708CA ILEB 33610.917 -1.087-16.7191.00 42.30 B C

ATOM 4709CB ILEB 33612.207 -1.808-16.2361.00 41.60 B C

ATOM 4710CG2ILEB 33613.421 -1.312-16.9991.00 40.56 B C

ATOM 4711CG1ILEB 33612.412 -1.531-14.7451.00 42.16 B C

ATOM 4712CD1ILEB 33613.434 -2.424-14.0811.00 41.61 B C

ATOM 4713C ILEB 33611.195 0.390 -17.0181.00 42.66 B C

ATOM 4714O ILEB 33611.105 1.233 -16.1251.00 41.54 B O

ATOM 4715N METB 33711.518 0.708 -18.2701.00 42.44 B N

ATOM 4716CA METB 33711.787 2.100 -18.6331.00 42.48 B C

ATOM 4717CB METB 33712.446 2.181 -20.0101.00 41.89 B C

ATOM 4718CG METB 33713.844 1.573 -20.0721.00 41.15 B C

ATOM 4719SD METB 33714.971 2.239 -18.8341.00 41.93 B 5 ATOM 4720CE METB 33714.930 3.986 -19.2281.00 42.22 B C

ATOM 4721C METB 33710.493 2.922 -18.6151.00 43.23 B C

ATOM 4722O METB 33710.513 4.121 -18.3281.00 43.07 B O

ATOM 4723N GLUB 3389.373 2.271 -18.9241.00 43.25 B N

ATOM 4724CA GLUB 3388.070 2.925 -18.8991.00 43.15 B C

ATOM 4725CB GLUB 3386.992 1.982 -19.4431.00 44.92 B C

ATOM 4_726CG GLUB 3385.642 2.654 -19.6801.00 48.81 B C

ATOM 4727CD GLUB 3384.518 1.664 -20.0071.00 50.80 B C

ATOM 4728OE1GLUB 3384.677 0.849 -20.9441.00 50.5 B O

ATOM 4729OE2GLUB 3383.468 1.707 -19.3251.00 _ B O
51.25 ATOM 4730C GLUB 3387.762 3.265 -17.4291.00 42.43 B C

ATOM 4731O GLUB 3387.221 4.322 -1%.1161.00 41.92 B O

ATOM 4732N GLUB 339-8.115 2.355 -16.5291.00 41.0 B N

ATOM 4733CA GLUB 33_9_7.883 2.572 -15.1101.00 _ B C
40.13 ATOM 4734CB GLUB 3398.117 1.269 -14.3331.00 39.57 B C

ATOM 4735CG GLUB 3397.458 1.235 -12.9701.00 38.75 B C

ATOM 4736CD GLUB 3_397.617 -0.106-12.2511.00 39.44 B C

ATOM 4737OE1GLUB 3397.161 -1.135-12.7991.0 38.03 B O

ATOM 4738OE2GLU8 3398.192 -0.124-11.135_ 37.25 B O
1.00 ATOM 4739C GLUB 3398.828 3.679 -14.6321.00 39.44 B C

ATOM 4740O GLUB 3398.415 4.609 -13 1.00 39.15 B 0 .931 ATOM 4741N PHEB 34010.095 3.592 _ 1.00 38.78 B N
-15.021 ATOM 4742CA PHEB 34011.054 4.616 -14.6331.00 39.52 B C

ATOM 4743CB PHEB 34012.434 4.326 -15.2351.00 40.84 B C

ATOM 4744CG PHEB 34013.171 3.200 -14.5561.00 44.13 B C

ATOM 4745CD1PHEB 34012.603 2.522 -13.4701.00 43.40 B C

ATOM 4746CD2PHEB 34014.441 2.823 -14.9931.00 43.94 B C

ATOM 4747CE1PHEB 34013.292 1.487 -12.8 1.00 45.13 B C

ATOM 4748CE2PHEB 34015.140 1.789 _ 1.00 45.26 B C

-14.361 ATOM 4749CZ PHEB 34014.567 1.120 -13.2801.00 45.08 B C

ATOM 4750C PHEB 34010.585 5.996 -15.0931.00 39.15 B C

ATOM 4751O PHEB 34010.574 6.951 -14.3211.00 38.55 B O

ATOM 4752N PHEB 34110.197 6.100 -1 1.00 38.55 B N
6.357 ATOM 4753CA PHEB 3419.748 7.374 _ 1.00 37.83 B C
-16.881 ATOM 4754CB PHEB 3419.504 7.274 -15.3931.00 38.07 B C

ATOM 4755CG PHEB 34110.751 7.005 -19.1921.00 38.34 B C

ATOM 4756CD1PHEB 34111.958 _7.611-18.8481.00 38.95 B C

ATOM 4757CD2PHEB 34110.714 6.173 -20.3141.00 39.95 B C

ATOM 4758CE1PHEB 34113.115 7.395 -19.6121.00 40.18 B C

ATOM 4759CE2PHEB 34111.863 5.949 -21.0881.00 39.79 B C

ATOM 4760CZ PHEB 34113.065 6.562 -20.7371.00 40.03 B C

ATOM 4761C PHEB 3418.489 7.846 -16.1621.00 37.20 B C

ATOM 4762O PHEB 3418.343 9.035 -15.8921.00 37.85 B O

ATOM 4763N ARGB 3427.575 6.936 -15.8421.00 35.80 B N

ATOM 4764CA ARGB 3426.384 7.375 -15.1461.00 36.10 B C

ATOM 4765CB ARGB 3425.351 6.251 -15.0181.00 39.67 B C

ATOM 4766CG ARGB 3424.535 6.086 -16.3121.00 47.06 B C

ATOM 4767CD ARGB 3423.225 5.310 -16.1361.00 52.95 B C

ATOM 4768NE ARGB 3423.397 3.860 -16.2491.00 58.03 B N

ATOM 4769CZ ARGB 3422.390 2.985 -16.2721.00 59.73 B C

ATOM 4770NHtARGB 3421.132 3.414 -16.1861.00 60.11 B N

ATOM 4771NH2ARGB 3422.641 1.683 -16.3911.00 59.56 B N

ATOM 4772C ARGB 3426.774 7.946 -13.7961.00 33.82 B C

ATOM 4773O ARGB 3426.233 8.968 -13.3881.00 31.87 B O

ATOM 4774N GLNB 3437.741 7.323 -13.1191.00 33.05 B N

ATOM 4775CA GLNB 3438.192 7.850 -11.8281.00 30.37 B C

ATOM 4776CB GLNB 3439.245 6.943 -11.1501.00 31.32 B C

ATOM 4777CG GLNB 3439.641 7.445 -9.7481.00 32.20 B C

ATOM 4778CD GLNB 34310.561 6.514 -8.9681.00 31.71 B C

ATOM 4779OE1GLNB 34310.301 5.323 -8.8681.00 32.36 B O

ATOM 4780__NE2GLNB 34311.630 7.070 -8.3851.00 29.06 B N

ATOM 4781C GLNB 3438.805 9.215 -12.1041.00 28.94 B C

ATOM 4782O GLNB 3438.575 10.166-11.3571.00 29.66 B O

ATOM 4783N GLYB 3449.567 9.316 -13.1901.00 25.85 B N

ATOM 4784CA GLYB 34410.195 10.582-13.5361.00 25.93 B C

ATOM 4785C GLYB 3449.207 11.716-13.7751.00 26.87 B C

ATOM 4786O GLYB 3449,446 12.854-13.3871.00 24.84 B O

ATOM 4787N ASPB 3458.091 11.404-14.A201.00 28.21 B N

ATOM 4788CA ASPB 3457.072 12.406-14.6801.00 29.67 B C

ATOM 4789CB ASPB 3455.979 11.852-15.6081.00 29.44 B C

ATOM 4790CG ASPB 3456.461 11.667-17.0331.00 31.36 B C

ATOM 4791OD1ASPB 3457.447 12.334-17.4201.00 28.47 B O

ATOM 4792OD2ASPB 3455.839 10.866-17.7681.00 32.54 B O

ATOM 4793C ASPB 3456.450 12.825-13.3621.00 30.07 B C

ATOM 4794O ASPB 3456.140 13.997-13.1631.00 29.40 B O

ATOM 4795N ARGB 3466.275 11.861-12.4631.00 31.09 B N

ATOM 4796CA ARGB 3465.684 12.135-11.1581.00 33.21 B C

ATOM 4797CB ARGB 3465.428 10.828-10.4141.00 34.34 B C

ATOM 4798CG ARGB 3464.413 9.947 -11.1171.00 35.78 B C

ATOM 4799CD ARGB 3463.357 9.524 -10.1401.00 39.73 B C

ATOM 4800NE ARGB 3463.496 8.131 -9.7301.00 42.71 B N

ATOM 4801CZ ARGB 3463.229 7.687 -8.5051.00 42.0 B C

ATOM 4802NH1ARGB 3462.821 8.529 -7.5611.00 _ B N
41.57 ATOM 4803NH2ARG~ 3463.344 6.396 -8.2341.00 41.42 B N
B

ATOM 4804C ARGB 3466.568 13.052-10.3261.00 34.40 B C

ATOM 48050 ARGB 3466.071 13.921-9.6221.00 34.97 B O

ATOM 4806N GLUB 3477.881 12.857-10.4151:00 35.57 B N

ATOM 4807CA GLUB 3478.824 13.687-9.6821.00 36.24 B C

ATOM 4808CB GLUE 34710.241 13.069-9.7231.00 36.37 B C

ATOM 4809CG GLUB 34710.324 11.623-9.1881.00 36.92 B C

ATOM 4810CD GLUB 34711.685 10.947-9.4061.00 37.18 B C

ATOM 4811OE1GLUB 34712.390 11.301-10.3691.00 37.68 B O

ATOM 4812OE2GLUB 34712.044 10.436-8.6271.00 38.18 B O

ATOM 4813C GLUB 3478.823 15.076-10.3351.00 37.37 B C

ATOM 4814O GLUB 3478.874 16.097-9.6531.00 36.50 B O

ATOM 4815N ARGB 3488.742 15.114-11.6611.00 38.88 B N

ATOM 4816CA ARGB 3488.743 16.395-12.3721.00 40.20 B C

ATOM 4817CB ARGB 3488.696 16.180-13.8881.00 40.25 B C

ATOM 4818CG ARGB 3489.432 17.260-14.7021 42.36 B C
.00 ATOM 4819CD ARGB 3489.071 17:196-16.194_ 42.24 B C
' _ 1.00 ATOM 4820NE ARGB 3489.163 15.836-16.7231.00 _ B N
43.13 ATOM 4821CZ ARGB 348_10.306 15.206-16.9551.00 44.34 B C

ATOM 4822NH1ARGB 34811.456 15.825-16.7131.00 46.11 B N

ATOM 4823NH2ARGB 34810.303 13.957-17.4071.00 41.29 B N

ATOM 4824C ARG8 3487.564 17.268-11.9441.00 40.17 B C

ATOM 4825O ARGB 3487.739 18.458-11.6981.00 40.10 B O

ATOM 4826N GLUB 3496.378 16.665-11 1.00 40.90 B N

ATOM 4827CA GLUB 3495.152 17.372_ 1.00 40.76 B C
-11.446 ATOM 4828CB GLUB 3493.953 16.432-11.3521.00 40.10 B C

ATOM 4829CG GLUB 3493.730 15.487-12.4731.00 41.96 B C

ATOM 4830CD GLUB 3492,592 14.540-12.1501.00 41.50 B C

ATOM 4831OE1GLUB 3492.585 14.009-11,0301.00 40.67 B O

ATOM 4832OE2GLUB 3491.712 14.322-13.0061.00 43.06 B O

ATOM 4833C GLUB 3495.285 17.983-10.0651.00 40.75 B C

ATOM 4834O GLUB 3494.709 19.025_ 1.00 41.56 B O
-9.773 ATOM 4835N ARGB 3506.020 17.301-9.2001.00 41.07 B N

ATOM 4836CA ARGB 3506.189 17.761-7.8361.00 40.88 B C

ATOM 4837CB ARGB 3506.279 16.552-6.9231.00 39.72 B C

ATOM 4838CG ARGB 3505.113 15.617-7.0841.00 39.18 B C

ATOM 4839CD ARGB 3505.488 14.210-6.6711.00 37.75 B C

ATOM 4840NE ARGB 3504.334 13.322-6.6801.00 36.32 B N

ATOM 4841CZ ARGB 3503.590 13_.072-5.5141.00 36.09 B C

ATOM 4842NHtARGB 3503.885 13.643-4 1.00 37.03 B N

ATOM 4843NH2ARGB 3502.560 12.244_ 1.00 39.08 B N
-5.696 ATOM 4844C ARGB 3507.407 18.645-7.6401.00 41.37 B C

ATOM 4845O ARGB 3507.697 19.055-6.5261.00 42.52 B 0 ATOM 4846N GLYB 3518.115 18.945-8.7171.00 42.06 B N

ATOM 4847CA GLYB 3519.300 1_9.770-8.5881.00 44.06 B C

ATOM 4848C GLYB 35110.408 19.070-7.8101.00 45.24 B C

ATOM 4849O GLYB 35111.299 19.729-7.2541.00 45.21 B O

ATOM 4850N METB 35210.352 17 -7 1 00 45 B N
~ - ~ ~ ~ ~ ~ 739 763 21 I

ATOM 4851CA METB 35211.363 16.942-7.0681.00 45.96 8 C

ATOM 4552CB METB 35210.805 15.581_ -6.6561.00 46.05 B C

ATOM 4853CG METB 3529.699 15.583-5.6311.00 45.39 B C

ATOM 4854SD METB 3528.935 13.946-5.5771.00 47.03 B S

ATOM 4855CE METB 35210.345 12.914-5.1721.00 47.69 B C

ATOM 4856C METB 35212.502 16.683-8.0341.00 47.50 B C

ATOM 48570 METB 35212.318 16.768-9.2501.00 48.46 B O

ATOM 4858N GLUB 35313.675 16.358-7.5001.00 48.62 B N

ATOM 4859CA GLUB 35314.819 16.043-8.3461.00 48.92 B C

ATOM 4860CB GLUB 35316.073 15.833-7.4881.00 50.87 B C

ATOM 4861CG GLUB 35317.357 15.635-8.2861.00 56.23 B C

ATOM 4862CD GLUB 35318.601 15.544-7.4021.00 59.66 B C

ATOM 4863OE7GLUB 35318.833 16.475-6.5921.00 61.59 B O

ATOM 4864OE2GLUB 35319.352 14.546-7.5201.00 61.43 B O

ATOM 4865C GLUB 35314.429 14.744-9.0611.00 47.81 B C

ATOM 4866O GLUB 35313.805 13.865-8.4571.00 46.04 B O

ATOM 4867N ILEB 35414.768 14.629-10.3411.00 47.09 B N

ATOM _48_68__CA fLEB 35414.418 13.432-11.0941.00 47.64 B C

ATOM 4869CB ILEB 35414.147 13.752-12.5811.00 47.93 B C

ATOM 4870CG2ILE8 35413.717 12.453-13.3201.00 46.29 B C

ATOM 4871CG1ILEB 35413.056 14.823-12.6961.00 48.54 B C

ATOM 4872CD1ILEB 35412.639 15.112-14.1301.00 48.80 B C

ATOM 4873C ILEB 35415.507 12.371-11.0151.00 48.37 B C

ATOM 4874O ILEB 35416.648 12.608-71.4001.00 48.77 B O

ATOM 4875N SERB 35515.137 11.195-10.5181.00 48.68 B N

ATOM 4876CA SERB 35516.061 10.082-10.3771.00 49.14 B C

ATOM 4877CB SERB 35515.311 8.872 -9.8231.00 47.86 B C

ATOM 4878OG SERB 35514.679 9.199 -8.6021.00 46.28 B O

ATOM 4879C SERB 35516.727 9.721 -11.7091.00 50.49 B C

ATOM 4880O SERB 35516.252 10.103-12.7831.00 51.13 B O

ATOM 4881N PROB 35617.840 8.974 -11.6531.00 51.57 B N

ATOM 4882CD PROB 35618.545 8.508 -10.4441.00 51.78 B C

ATOM 4883CA PROB 35618.557 8.572 -12.8721.00 51. B C

ATOM 4884CB PROB 35619.803 7.866 -12.3321.00 _ B C
52.22 ATOM 4885CG PROB 35619.968 8.429 -10.9261.00 52.71 B C

ATOM 4886C PROB 35617.703 7.629 -13.7181.00 52.39 B C

ATOM 4887O PROB 35616.910 6.854 -13.1801.00 52.97 B O

ATOM 4888N METB 35717.866 7.696 -15.0361.00 51 B N
.63 ATOM 4889CA METB 35717.125 6.831 -15.9521.00 51.35 B C

ATOM 4890CB METB 35717.307 5.348 -15.5841.00 53.37 B C

ATOM 4891CG METB 35718.743 4.860 -15.4331.00 54.59 B C

ATOM 4892SD MET8 35718.809 3.051 -15.2281.00 _ B S
57.29 ATOM 4893CE METB 35718.365 2.859 -13.4961.00 56.75 B C

ATOM 4894C METB 35715.630 7.120 -15.9771.00 50.18 B C

ATOM 4895O METB 35714.903 6.562 -16.799_ 50.00 B O
1.00 ATOM 4896N CYSB 35815.162 7.985 -15.0861.00 48.99 B N

ATOM 4897CA CYSB 35813.740 8.278 -15.0381.00 48.29 B C

ATOM 4898CB CYSB 35813.292 8.413 -13.5771.00 48.01 B C

ATOM 4899SG CYSB 35813.430 6.873 -12.6211.00 46.22 B S

ATOM 4900C CYSB 35813.308 9.503 -15.8321.00 47.97 B C

ATOM 4901O CYSB 35812.11 9.790 -15.9271.00 _ B O
S 47.56 ATOM 4902N ASPB 35914.265 10.215-16.4151.00 48.41 B N

ATOM 4903CA ASPB 35913.948 11.418-17.1811.D0 49.64 B C

ATOM 4904CB ASPB 35915.005 12.494-16.9001.00 48.73 B C

ATOM 4905CG ASPB 35914.684 13.823-17.5711.00 49.39 B C

ATOM 4906OD1ASPB 35913.624 13.925-18.2351.00 47.41 B 0 ATOM 4907OD2ASPB 35915.498 14.766-17.4301.00 48.72 B O

ATOM 4908C ASPB 35913.845 11.136-18.685__ 50.20 B C
1.00 ATOM 49090 ASPB 35914.853 11.021-19.3791.00 50.28 B O

ATOM 4910N LYSB 36012.618 11.034-19 1.00 51.59 B N
.181 ATOM 4911CA LYSB 36012.383 10.745_ 1.00 53.77 B C
-20.590 ATOM 4912CB LYSB 36010.893 10.505-20.8431.00 53.00 B C

ATOM 4913CG LYSB 36010.008 11.731-20.638__ 53.92 B C
1.00 ATOM 4914CD LYSB 3608.535 11.348-20.7541.00 54.67 B C

ATOM 4915CE LYSB 3607.608 12.524-20.4821.00 54.41 B C

ATOM 4916NZ LYSB 3606.173 12.104-20.4951.00 54.32 B N

ATOM 4917C LYSB 36012.882 11.825-21.5441.00 55.46 B C

ATOM 4918O LYSB 36012.723 11.693-22.7551.00 56.58 B O

ATOM 4919N HISB 36113.477 12.889-21.0111.00 56.48 B N

ATOM 4920CA HISB 36113.986 13.968-21.8531.00 57.52 B C

ATOM 4921CB HISB 36113.503 15.324-21.3401.00 56.40 B C

ATOM 4922CG HISB 36112.017 15.482-21.3671.00 56.13 B C

ATOM 4923CD2HISB 36111.143 15.879-20.4101.00 56.34 B C

ATOM 4924ND1HISB 36111.263 15.232-22.4941.00 55.87 B N

ATOM 4925CE1HISB 3619.990 _ -22.2321.00 56.03 B C

15.469 ATOM 4926NE2HISB 3619.890 15.563-20.9741.00 56.50 B N

ATOM 4927C HIS8 36115.509 13.950-21.9131.00 59.07 B C

ATOM 4928O HISB 36116.110 14.586-22.7791.00 60.01 B O

ATOM 4929N ASNB 36216.125 13.233-20.9771.00 59.87 B N

ATOM 4930CA ASNB 36217.577 13.094-20.9281.00 60.87 B C

ATOM 4931CB ASNB 36278.162 13.852-19.7331.00 62.13 B C

ATOM 4932CG ASNB 36218.084 15.363_ 1.00 63.63 B C
-19.895 ATOM 4933OD1ASNB 36219.050 16.076-19.6081.00 64.26 B O

ATOM 4934ND2ASNB 36216.933 15.860-20.3381.00 64.37 B N

ATOM 4935C ASNB 36217.895 11.604-20.7931.00 60.58 B C

ATOM 4936O ASNB 36218.831 11.210-20.0941.00 61.51 B O

ATOM 4937N ALAB 363_ 17.10410.787 -21.4801.00 59.58 B N

ATOM 4938CA ALAB 36317.2459.337 -21.4451.00 58.36 B C

ATOM 4939CB ALA8 36315.9498.689 _ -21.9251.00 58.79 B C

ATOM 4940C ALAB 36318.4228.788 -22.2461.00 57.23 B C

ATOM 4941O ALAB 36318.9059.412 -23.1901.00 57.39 B O

ATOM 4942N SERB 36418,8687.604 -21.8471.00 55.54 B N

ATOM 4943CA SERB 36419.9736.905 -22.4891.00 54.79 B G

ATOM 4944CB SERB 36421.3047.254 -21.8131.00 56.05 B C

ATOM 4945OG SERB 36421.4138.642 -21.5391.00 57.70 B O

ATOM 4946C SERB 36419.6585.434 -22.2551.00 53.69 B C

ATOM 4947O SERB 36420.5094.665 -21.8 1.00 54.06 B O

ATOM 4948N VALB 36518.4195.060 _ 1.00 51.55 B N
_ -22.551 ATOM 4949CA VALB 36517.9513.700 -22.3591.00 50.38 B C

ATOM 4950CB VALB 36516.6933.447 -23.2041.00 49.08 B C

ATOM 4951CG1VALB 36516.2621.999 -23.0881.00 48.32 B C

ATOM 4952CG2VALB 36515.5744.363 -22.7341.00 48.72 B C

ATOM 4953C VALB 36519.0062.640 -22.6681.00 50.94 B C

ATOM 4954O VALB 36519.1771.691 -21.8981.00 50.33 B O

ATOM 4955N GLUB 36619.7172.807 -23.7831.00 51.43 B N

ATOM 4956CA GLUB 36620.7511.857 -24.1791.00 52.12 B C

ATOM 4957CB GLUB 36621.158_ -25.6381.00 53.43 B C
2.065 ATOM 4958CG GLUB 36620.0811.684 -26.6251.00 55.14 B C

ATOM 4959CD GLUB 36619.0732.790 -26.8481.00 56.23 B C

ATOM 4960OE1GLUB 36617.9372.468 -27.2621.00 58.18 B 0 ATOM 4961OE2GLUB 36619.4193.974 -26.625_1.00 55.44 B O

ATOM 4962C GLUB 36621.9871.940 -23.3021.00 51.91 B C

ATOM 4963O GLUB 36622.4680.918 -22.8161.00 51.27 B O

ATOM _49_64N LYSB 36722.506' 3.149-23.1061.00 51.89 B N

ATOM 4965CA LYSB 36723.6843.320 -22.2661.00 53.09 B C

ATOM 4966CB LYSB 36724.0674.794 -22.1351.00 55.30 B C

ATOM 4967CG LYSB 36724.8955.358 -23.2761.00 59.08 B C

ATOM 4968CD LYSB 36725.3916.767 -22.9311.00 61.56 B C

ATOM 4969CE LYSB 36726.2207.386 -24.0621.00 63.61 B C

ATOM .4970NZ LYSB 36726.7178.761 -23.7171.00 63.66 B N

ATOM 4971C LYSB 36723.4002.765 -20.8811.00 52.67 B C

ATOM 4972O LYSB 36724.3142.319 -20.1861.00 53.33 B O

ATOM 4973N SERB 36822.1302.795 -20.4841.00 51.46 B N

ATOM 4974CA SERB 36821.7322.302 -19.1751.00 50.43 B C

ATOM 4975CB SERB 36820.3202.781 -18.8251.00 49.24 B C

ATOM 4976OG SERB 36820.3024.175 -18.6111.00 48.85 B O

ATOM 4977C SERB 36821.7830.782 -19.0951.00 50.41 B C

ATOM 4978O SERB 36822.2440.226 -18.0951.00 49.92 B O

ATOM 4979N GLNB 36921.2980.110 -20.1381.00 49.16 B N

ATOM 4980CA GLNB 36921.305-1.343 -20.147_ _ B C
1.00 47.89 ATOM 4981CB GLNB 36920.606-1.870 -21.3951.00 48.02 B C

ATOM 4982CG GLNB 36919.107-1.576 -21.4101.00 48.99 B C

ATOM 4983CD GLNB 36918.418-1.990 -20.1121.00 49.83 B C

ATOM 4984OE1GLNB 36918.499-3.144 -19.6931.00 49.48 B O

ATOM 4985NE2GLNB 36917.737-1.042 -19.4721.00 49.46 B N

ATOM 4986C GLNB 36922.734-1.853 -20.0821.00 47.51 B C

ATOM 4987O GLNB 36923.038-2.794 -19.3531 46.66 B O
.00 ATOM 4988N VALB 37023.618-1.215 -20.837_ 47.02 B N
1.00 ATOM 4989CA VALB 37025.015-1.613 -20.8351.00 46.39 B C

ATOM 4990CB VALB 37025.818-0.839 -21.9001.00 46.62 B C

ATOM 4991CG9VALB 37027.296-1.210 -21.8011.00 45.44 B C

ATOM 4992CG2VALB 37025.263-1.146 -23.2971.00 44.05 B C

ATOM 4993C VALB 37025.608-1.337 -19.4611.00 46,00 B C

ATOM 4994O VALB 37026.308-2.180 -18.9031.00 47.24 B O

ATOM 4995N GLYB 37125.323-0.154 -18.9191.00 44.48 B N

ATOM 4996CA GLYB 37125.8360.197 -17.6071.00 42.29 B C

ATOM 4997C GLYB 37125.339-0.778 -16.5571.00 41.72 B C

ATOM 4998O GLYB 37126.097-1.244 -15.7041.00 40.44 B O

ATOM 4999N PHEB 37224.052-1.096 -1 1.00 41.34 B N
6.632 ATOM 5000CA PHEB 37223.432-2.016 _ 1.00 40.50 B C
-15.696 ATOM 5001CB PHEB 37221.936-2.119 -15.9951.00 37.63 B C

ATOM 5002CG PHEB 37221.175-2.961 -15.0081.00 36.02 B C

ATOM 5003CD1PHE8 37221.364-2.796 -13.6411.00 35.43 B C

ATOM 5004CD2PHEB 37220.267-3.911 -15.4451.00 34.47 B C

ATOM 5005CE1PHEB 37220.661-3.566 -12.7331,00 35.07 B C

ATOM 5006CE2PHEB 37219.563-4.682 -14.5431.00 34.58 B C

ATOM 5007CZ PHEB 37219.761-4.511 -13.1831.00 34.09 B C

ATOM 5008C PHEB 37224.087-3.394 -15.7771.00 42.09 B C

ATOM 5009O PHEB 37224.365-4.026 -14.7461.00 41.48 B O

ATOM 5010N ILEB 37324.338-3.852 -17.0021.00 42.94 B N

ATOM 5011CA ILEB 37324.966-5.154 -17.2101.00 44.87 B C

ATOM 5012CB ILEB 37324.873-5.605 -18,6961.00 45.22 B C

ATOM 5013CG2ILEB 37325.734-6.843 -18.9251.00 46.17 B C

ATOM 5014CG1ILEB 37323.414-5.930 -19.0471.00 . 46.37B C

ATOM 5015CD1ILEB 37323.187-6.350 -20.4901.00 46.17 B C

ATOM 5016C ILEB 37326.430-5.175 -16.7691.00 45.17 B C

ATOM 5017O ILEB 37326.877-6.144 -16.1561.00 45.07 B O

ATOM 5018N ASPB 37427.171-4.109 -17.0551.00 45.73 B N

ATOM 5019CA ASPB 37428.580-4.065 -16.6701.00 47.29 B C

ATOM 5020CB ASPB 37429.311-2.923 -17.3841.00 48.13 B C

ATOM 5021CG ASPB 37429.587-3.229 -18.8501.00 49.76 B C

ATOM 5022OD1ASPB 37429.692-4.428 -19.2001.00 49.02 B O

ATOM 5023OD2ASPB 37429.714-2.268 ~ -19.6461.00 50.78 B O
ATOM 5024C ASP8 37428.850-3.961 -15.1731.00 47.49 B C
ATOM 5025O ASPB 37429.695-4.683 -14.6391,00 47.87 B O
ATOM 5026N TYRB 37528.137-3.075 -14.4891.00 47.72 B N
ATOM 5027CA TYRB 37528.368-2.903 -13.0611.00 48.07 B C
ATOM 5028CB TYRB 37528.096-1.456 -12.6461,00 49.34 B C
ATOM 5029CG TYRB 37529.038-0.464 -13.2771.00 52.89 B C
ATOM 5030CDiTYRB 37528.879-0.067 -14.6091.00 54.75 B C
ATOM 5031CE1TYRB 37529.7590.842 -15.2001.00 56.67 B C
ATOM 5032CD2TYRB 37530.1010.070 -12.5511.00 53.98 B C
ATOM 5033CE2TYRB 37530.9880.978 -13.1291.00 55.74 B C
ATOM 5034CZ TYRB 37530.8151.361 -14.4521.00 56.91 B C
ATOM 5035OH TYRB 37531.6942.259 -15.0221.00 57.12 B O
ATOM 5036C TYRB 37527.599-3.834 -12.1341.00 46.59 8 C
ATOM 5037O TYRB 37528.005.4.022 -10.9911.00 46.33 B O
ATOM 5038N iLEB 37626.516-4.436 -12.6151.00 44.77 B N
ATOM 5039CA ILEB 37625.733-5.299 -11.7481:00 44.37 B C
ATOM 5040CB ILEB 37624.465x.534 -11.2811.00 44.69 B C
ATOM 5041CG2ILEB 37623.461-5.480 -10.6211.00 43.80 B C
ATOM 5042CG1ILEB 37624.8933.408 -10.3401.00 43.74 B C
ATOM 5043CD1ILEB 37623.779-2.545 -9,8711.00 45.65 B C
ATOM 5044C ILEB 37625.342-6.694 -12.2571.00 44.94 B C
ATOM 5045O ILEB 37625.705-7.707 -11.6471.00 45.08 B O
ATOM 5046N VALB 37724.614-6.765 -13.3621.00 43.75 B N
ATOM 5047CA VALB 37724.186-8.062 -13.8531.00 45.05 B C
ATOM 5048C8 VALB 37723.259-7,905 -15.0481.00 43.53 B C
ATOM 5049CGtVALB 37722.742-9.264 -15.4871.00 42.29 B C
ATOM 5050CG2VALB 37722.109-6.976 -14.6721.00 42.92 B C
ATOM 5051C VALB 37725.312-9.029 -14.2131.00 47.43 B C
ATOM 5052O VALB 37725.236-10.220-13.9031.00 47.23 B O
ATOM 5053N HISB 37826.3608.528 -14.8561.00 49.44 B N
ATOM 5054CA HISB 37827.463-9.396 -15,2411.00 51.40 B C
ATOM 5055CB HISB 37828.389-8,694 -16.2481.00 52.82 B C
ATOM 5056CG H!SB 37829,417-9.602 -16.8461.00 54.77 B C
ATOM 5057CD2HISB 37829.390-10.357-17.9721.00 55.31 B C
ATOM 5058ND1HISB 3783p.605-9.902 -16.2121.00 55.6.1B N
ATOM 5059CE7HISB 37831.260-10.807-16.9191.00 56.42 B C
ATOM 5060NE2HISB 37830.544-11.101-17.9901.00 55.35 B N
ATOM 5061C HISB 37828.257-9.871 -14.0251.00 51.27 B C
ATOM 5062O HISB 37828.443-11.071-13.8361.00 50.92 B O
ATOM 5063N PROB 37928.739-8.940 -13.1831.00 51.45 B N
ATOM 5064CD PROB 37928.778-7.472 -13.3131.00 51.09 B C
ATOM 5065CA PROB 37929.498-9.375 -12.0071.00 51.08 B C
ATOM 5066CB PROB 37929.774-8.067 -11.2771.00 49.65 B C
ATOM 5067CG PROB 37929.941-7.106 -12.4091.00 50.48 B C
ATOM 5068C PROB 37928.723-10.377-11.1471,00 51.13 B C
ATOM 5069O PROB 37929.317-11.263-10.5421.00 52.44 B O
ATOM 5070N LEUB 38027.401-10.245-11.0931.00 51.30 B N
ATOM 5071CA LEUB 38026.59211.173 -10.3041.00 50.72 B C
ATOM 5072CB LEUB 38025.157-10.649-10.1181.00 45.98 B C
ATOM 5073CG LEUB 38024.126-11.616-9.4991.00 47.87 B C
ATOM 5074CD1LEU8 38024,630-12.101-8.1501.00 46.39 B C
ATOM 5075CD2LEU8 38022.767-10.928-9.3381.00 45.58 B C
ATOM 5076C LEUB 38026.551-12.527-11.0011.00 51.27 B C
ATOM 5077O LEUB 38026.875-13.559-10.4041.00 50.55 B O
ATOM 5078N TRPB 38126.160-12,519-12,2701.00 51.45 B N
ATOM 5079CA TRPB 38126.071-13,754-13,0341.00 53.13 B C
ATOM 5080CB TRPB 38125.294-13.514-14.3201.00 53.25 B C
ATOM 5081CG TRPB 38123.843-13.534-14.0701.00 54.09 B C
ATOM 5082CD2TRPB 38123.004-14.693-14.0351.00 54.05 B C
ATOM 5Q83CE2TRPB 38121.703-14.257-13.7061.00 53.73 B C
ATOM 5084CE3TRPB 38123.227-16.061-14.2481.00 54.33 B C
ATOM 5085CD1TRPB 38123.046-12.470-13.7691.00 53.28 g C
ATOM 5086NEiTRPB 38121.757-12,895-13.5521.00 54.16 B N
ATOM 5087CZ2TRPB 38120.624-15.138-13.5861.00 53.17 B C
ATOM 5088CZ3TRPB 38122.151-16.942-14.1291.00 54.44 B C
ATOM 5089CH2TRPB 38120.866-16.472-13,8001.00 54.33 B C
ATOM 5090C TRPB 38127.400-14.428-13.3521.00 53.50 B C
ATOM 50910 TRPB 38127.443-15.620-13.6261.00 53.16 B O
ATOM 5092N GLUB 38228.482-13.665-13.3101.00 54.29 B N
ATOM 5093CA GLUB 38229.796-14.209-13.5901.00 55.12 B C
ATOM 5094CB GLUB 38230.812-13.068-13.7091.00 56.79 B C
ATOM 5095CG GLUB 38232.243-13.500-13.9441.00 58.61 B C
ATOM 5096CD GLUB 38233.153-12.318-14.2311.00 60.80 B C
ATOM 5097OE1GLUB 38233.176-11.377-13.4021.00 61.51 B 0 ATOM 5098OE2GLUB 38233.840-12.330-15.2811.00 60.49 B O
ATOM 5099C GLUB 38230.166-15.124-12,4341.00 55.03 B C
ATOM 5100O GLUB 38230.864-16.127-12.6051.0p 54.63 B 0 ATOM 5101N THRB 38329.675-14.780-11.2501.00 54.00 B N
ATOM 5102CA THRB 38329.981-15.562-10.0671.00 52.85 B C
ATOM 5103CB THRB 38329.961-14.677-8,8191.00 51.09 B C
ATOM 5104OGtTHRB 38330.901-13.608-8.8881.0p 49.44 B 0 ATOM 5105CG2THRB 38330.334-15.483-7.5951.00 50.36 B C
ATOM 5106C THRB 38329.048-16.750-9.8671.00 53.17 B C
ATOM 5107O THRB 38329.480-17.801-9.3991.00 52.84 B O
ATOM 5108N TRPB 38427.774-16.594-10.2111.00 53.45 B N

ATOM 5109CA TRPB 38426.840-17.70010.0441.00 53.95 B C

ATOM 5110CB TRPB 38425.400-17.248-10.2991.00 50.96 B C

ATOM 5111CG TRPB 38424.405-18.371-10.1691.00 48.62 B C

ATOM 5112CD2 TRPB 38423.890-18.923-8.9521.00 47.80 B C

ATOM 5113CE2 TRPB 38423.004-19.966-9.3101.00 47.75 B C

ATOM 5114CE3 TRPB 38424.092-18.638-7.5941.00 47.86 B C

ATOM 5115CD1 TRPB 38423.825-19.083-11.1871.00 47.81 B C

ATOM 5116NE1 TRPB 38422.984-20.039-10.6791.00 47.52 8 N

ATOM 5117CZ2 TRPB 38422.314-20.724-8.3561.00 46.92 B C

ATOM 5118CZ3 TRPB 38423.406-19.390-6.6441.00 47.33 B C

ATOM 5119CH2 TRPB 38422.527-20.424-7.0331.00 48.04 B C

ATOM 5120C TRPB 38427.211-18.840-10.9941.00 55.37 B C

ATOM 5121O TRPB 38427.063-20.017-10.6571.00 55.86 B O

ATOM 5122N ALAB 38527.696-18.486-12.1811.00 56.99 B N

ATOM 5123CA ALAB 38528.113-19.480-13.1641.00 58.14 B C

ATOM 5124CB ALAB 38528.514-18.795-14.4691.00 56.72 B C

ATOM 5125C ALAB 38529.297-20.248-12.5701.00 59.14 B C

ATOM 5126O ALAB 38529.449-21.447-12.8071.00 59.12 B O

ATOM 5127N ASPB 38630.127-19.542-11.7991.00 60.62 B N

ATOM 5128CA ASPB 38631.288-20.136-11.1311.00 62.42 B C

ATOM 5129CB ASPB 38632.016-19.092-10.2771.00 62.67 B C

ATOM 5130CG ASPB 38633.114-18.381-11.0271.00 63.59 B C

ATOM 5131OD1 ASPB 38633.018-18.286-12.2681.00 64.60 B O

ATOM 5132OD2 ASPB 38634.070-17.905-10.3711.00 63.65 B O

ATOM 5133C ASPB 38630.811-21.248-10.2111.00 63.48 B C

ATOM 5134O ASPB 38631.233-22.402-10.3261.00 63.45 B O

ATOM 5135_N LEUB 38729.924-20.874-9.2961.00 64.32 B N

ATOM 5136CA LEUB 38729.363-21.792-8.3181.0D 66.14 B C

ATOM 5137CB LEUB 38728.331-21.063-7.4571.00 66.43 B C

ATOM 5138CG LEUB 38727.814-21,843-6.2481.00 66.82 B C

ATOM 5139CD1 LEUB 38728.939-21.997-5.2311.00 66.57 B C

ATOM 5140CD2 LEUB 38726.633-21.110-5.6271.00 67.78 B C

ATOM 5141C LEUB 38728.720-23.034-8.9291.00 66.87 B C

ATOM 5142O LEUB 38728.832-24.124-8.3731.00 67.44 B O

ATOM 5143N VALB 38828.040-22.874-10.0621.00 67.61 B N

ATOM 5144CA VALB 38827.381-24.003-10.7181.00 67.96 B C

ATOM 5145CB VALB 38825.880-23.699-10.9981.00 68.03 B C

ATOM 5146CG1 VALB 38825.173-23.337-9.7061.00 67.62 B C

ATOM 5147CG2 VALB 38825.746-22.572-12.0101.00 67.64 B C

ATOM 5148C VALB 38828.059-24.368-12,0361.00 68.35 8 C

ATOM 5149O VALB 38827.396-24.740-13.0011.00 67.41 B 0 ATOM 5150N HISB 38929.384-24.262-12.0691.00 69.38 B N

ATOM 5151CA HISB 38930.153-24.570-13.2721.00 70.70 B C

ATOM 5152CB HISB 38931.651-24.410-12.9871.00 71.50 B C

ATOM 5153CG HISB 38932.466-24.075-14.1981.00 72.79 B C

ATOM 5154CD2 HISB 38933.266-23.015-14.4671.00 73.38 B C

ATOM 5155ND1 HISB 38932.514-24.883-15.3141.00 _ B N
73.43 ATOM 5156CE1 HISB 38933.309-24.337-16.2191.00 73.57 B C

ATOM 5157NE2 HISB 38933.778-23.203-15.7291.00 74.29 B N

ATOM 5158C HISB 38929.867-25.994-13.7501.00 70. B C

ATOM 5159O HISB 38930.047-26.952-12.9981.00 _ B O
70.24 ATOM 5160N PROB 39029.430-26.155-15.0121.00 71.32 B N

ATOM 5161CD PROB 390_29.564-27.472-15.6651.00 71.78 B C

ATOM 5162CA PROB 39029.179-25.128-16.0281.00 71.81 B C

ATOM 5163CB PROB 39029.955-25.660-17.2161.00 72.07 B C

ATOM 5164CG PROB 39029.558-27.119-17.1721.00 71.68 B C

ATOM 5165C PROB 39027.689-25.023-16.3521.00 72.08 B C

ATOM 5166O PROB 39027.315-24.638-17.4611.00 71.66 B O

ATOM 5167N ASPB 391_26.853-25.391-15.3861.00 72.73 B N

ATOM 5168CA ASPB 39125.400-25.363-15.5461.00 72.93 B C

ATOM 5169CB ASPB 391_24.727-25.455-14.1751.00 74.36 B C

ATOM 5170CG ASPB 39125.153-26.687-13.3931.00 75.18 B C

ATOM 5171OD1 ASPB 39126.373-26.948__ _ 76.05 B O
-13.3 1.00 ATOM 5172OD2 ASPB 39124.266-27.387_ 1.00 74.61 B O
-12.862 ATOM 5173C ASPB 39124.929-24.096-16.2521.00 72.41 B C

ATOM 5174O ASPB 39124.102-24.149-1 1.00 71.49 B O
7.

ATOM 5175N ALAB 39225.462-22.961_ 1.00 72.10 B N
_ -15.

ATOM 5176CA ALAB 39225.102-21.670_ 1.00 72.39 B C

-16.385 ATOM 5177CB ALAB 39224.736-20.691-15.2771.00 72.34 B C

ATOM 5178C ALAB 39226.259-21.124-17.1971,00 72.19 B C

ATOM 5179O ALAB 39227.207-20.558-16.6461.00 72.61 B O

ATOM 5180N GLNB 39326.182-21.315-18.5081.00 71.53 B N

ATOM 5181CA GLN8 39327.211-20.841-19.4221.00 70.54 B C

ATOM 5182CB GLNB 39328.104-21.998- 1.00 70.45 B C
19.8 ATOM 5183CG GLNB 39329.305-21.553_ 1.00 70.44 B C
_ -20.707 ATOM 5184CD GLNB 39330.172-20.544-19.9681.00 70.88 B C

ATOM 5185OE1 GLNB 39330.634-20.804-18.8541.00 71.24 B O

ATOM 5186NE2 GLNB 39330.396-19.387-20.5851.00 70.16 B N

ATOM 5187C GLNB 39326.479-20.247-20.6081.00 69.76 B C

ATOM 5188O GLN8 39326.842-19.186-21.1121.00 69.64 B O

ATOM 5189N ASPB 39425.442-20.952-21.p471.00 68.66 B N

ATOM 5190CA ASPB 39424.622-20.502-22.1581.00 68.30 B C

ATOM 5191CB ASPB 39423.568-21.556-22.4851.00 69.69 B C

ATOM'5192CG ASPB 39424.177-22.908-22.7701.00 70.87 B C

ATOM 5193OD1 ASPB 39424.737-23.076-23.8761.00 70.49 B O

I 5194OD2 ASPB 39424.106-23 -21 1 OD 71 B (7 ATOM ~ ~ ~ ~ ~ ~ 793 882 62 ~

ATOM5195C ASPB 39423.947 -19.229-21.6761.00 67.49 B C

ATOM5196O ASPB 39423.745 -18.283-22.4421.00 66.71 B O

ATOM5197N ILEB 39523.600 -19.224-20.3901.00 66,07 B N

ATOM5198CA !LEB 39522.969 -18.073-19.7711.00 64.53 B C
ATOM5199CB ILEB 39522.608 -18.361-18.2961.00 64.15 B C
ATOM5200CG2ILE' 39522.118 -17.097-17.617' 63,76 8 C
B 1.00 ATOM5201CG1ILE. 39521.530 -19.442-18.2301.00 63.66 B C
B

ATOM5202CD1ILEB 39521.042 -19.723-16.8391.00 62.37 B C

ATOM5203C ILE~ 39523.950 -16.905-19.8331.00 63.65 B C
B

ATOM5204O ILE; 39523.636 -15.847-20.3831.00 63.76 B O
B

ATOM5205N LEUB 39625.145 -17.111-19.2861.00 62.01 B N

ATOM5206CA LEUB 39626.173 -16.076-19.2781.00 60.14 B C

ATOM5207CB LEU!.39627.453 -16.607-18.6321.00 59.92 B C
B

ATOM5208CG LEUB 39628.360 -15.574-17.9531.00 59.63 B C

ATOM5209CD1LEU. 39629.628 -16.267-17.4841.00 58.94 B C
B

ATOM5210CD2LEUB 39628.694 -14.440-18.9061.00 59.49 B C

ATOM5211C LEU, 39626.480 -15.593-20.6941.00 59.39 B C
B

ATOM5212O LEUB 39626.637 -14.396-20.9251.00 58.45 B O

ATOM5213N ASP~ 39726.567 -16.529-21.6361.00 59.02 B N
B

ATOM5214CA ASPB 39726.858 -16.189-23.0241.00 58.76 B C

ATOM5215CB ASP, 39727.081 -17.458-23.8621.00 59.93 B C
B

ATOM5216CG ASPB 39728.500 -18.004-23.7331.00 61.23 B C

ATOM5217OD1ASPB 39729.456 -17.225-23.9421.00 61.71 B O

ATOM5218002ASPB 39728.665 -19.206-23.4321.00 61.91 B 0 ATOM5219C ASPB 39725.755 -15.338-23.6411.00 57.94 B C

ATOM5220O ASPB 39726.039 -14.406-24.3931.00 57.81 B O

ATOM5221N THRB 39824.503 -15.659-23.3321.00 56.80 B N

ATOM5222CA THRB 39823.386 -14.879-23.8521.00 56.69 B C

ATOM5223CB THRB 39822.012 -15.444-23.4011.00 57.16 B C

ATOM5224OG1THRB 39821.878 -16.808-23.8241.00 56.47 B O

ATOM5225CG2THRB 39820.883 -14.627-24.0031.00 56.81 B C

ATOM5226C THRB 39823.532 -13.463-23.2971.00 56,53 B C

ATOM5227O THRB 39823.294 -12.488-24.0051.00 56.29 B O

ATOM5228N LEUB 39923.941 -13.363-22.0331.00 55.75 B N
-ATOM5229CA LEUB 39924.127 -12.071-21.3811.00 56.02 B C

ATOM5230CB LEUB 39924.582 -12.254-19.9291.00 54.57 B C

ATOM5231CG LEUB 39924.627 -90.950-19.1251.00 53.85 B C

ATOM5232CD1LEUB 39923.210 -10.371-19.0251.00 52.45 B C

ATOM5233CD2LEUB 39925.207 -11.199-17.7471.00 52.66 B C

ATOM5234C LEUB 39925.147 -11.201-22.1171.00 56.92 B C

ATOM5235O LEUB 39924.882 -10.032-22.4111.00 56.98 B O

ATOM5236N GLUB 40026.318 -11.764-22.4001.00 57.84 B N

ATOM5237CA GLUB 40027.354 -11.023-23.1101.00 58.35 B C

ATOM5238CB GLUB 40028.665 -11.825-23.1201.00 59.39 B C

ATOM5239CG GLUB 40029.481 -11.650-21.8251.00 60.70 B C

ATOM5240CD GLUB 40030.118 -12.942-29.3141.00 61.41 B C

ATOM5241OE1GLUB 40030.780 -12.901-20.2521.00 60.58 B O

ATOM5242OE2GLUB 40029.958 -13.999-21.9641.00 62.28 B O

ATOM5243C GLU8 40026.891 -10.674-24.5281.00 57.46 B C

ATOM5244O GLU8 40027.223 -9.607-25.0471.00 57.09 B O

ATOM5245N ASPB 40126.107 -11.559-25.1431.00 56.88 B N

ATOM5246CA ASPB 40125.584 -11.296-26.4831.00 56.54 B C

ATOM5247CB ASPB 40124.896 -12.533-27.0771.00 58.16 B C

ATOM5248CG ASPB 40125.875 -13.504-27.7201.00 59.79 B C

ATOM5249OD1ASPB 40126.813 -13.043-28.4091.00 60.41 B O

ATOM5250OD2ASPB 40125.692 -14.730-27.5551.00 60.56 B O

ATOM5251C ASPB 40124.569 -10.162-26.3941.00 55.73 B C

ATOM5252O ASPB 40124.647 -9.193-27.1521.00 56.25 B O

ATOM5253N ASNB 40223.619 -10.288-25.4631.00 53.95 B N

ATOM5254CA ASNB 40222.592 -9.269-25.2641.00 51.89 B C

ATOM5255CB ASNB 40221.628 -9.673-24.1471.00 51.10 B C

ATOM5256CG ASNB 40220.616 -10.716-24.5971.00 51.72 B C

ATOM5257OD1ASNB 40220.238 -10.769-25.7711.00 52.31 B O

ATOM5258ND2ASNB 40220.156 -11.540-23.6611.00 50.93 B N

ATOM5259C ASNB 40223.204 -7.903-24.9581.00 50.98 B C

ATOM5260O ASNB 40222.666 -6.877-25.3681.00 50.48 B 0 ATOM5261N ARGB 40324.325 -7.880-24.2471.00 50.91 B N

ATOM5262CA ARGB 40324.979 -6.611-23.9511.00 50.84 B C

ATOM5263CB ARGB 40326.199 -6.803-23.0551.00 51.07 B C

ATOM5264CG ARGB 40327.034 -5.535-22.9341.00 50.52 B C

ATOM5265CD ARGB 40328.358 -5.798-22.2451.00 51.78 B C

ATOM5266NE ARGB 40329.123 -4.570-2 1.00 51.23 B N
2.017 ATOM5267CZ ARGB 40329.626 -3.805_ 1.00 50.65 B C
-22.980 ATOM5268NH1ARGB 40329.449 -4.134-24.2541.00 51.42 B N

ATOM5269NH2ARGB 40330.3_07-2.712-22.6661.00 49.29 B N

ATOM5270C ARGB 40325.435 -5.984-25.2601.00 51.05 B C

ATOM5271O ARG8 40325.304 -4.779-25.4571.00 50.43 B 0 ATOM5272N GLUB 40425.984 -6.812-26.1461.00 51.31 B N

ATOM5273CA GLUB 40426.454 -6.338-27.4401.00 51.82 B C

ATOM5274CB GLUB 40427.091 -7.482-28.2471.00 54.01 B C

ATOM5275CG GLUB 40428.533 -7.814-27.8761.00 55.99 B C

ATOM5276CD GLUB 40429.425 -6.584-27,8391.00 56.59 B C

ATOM5277OE1GLUB 40429.494 -5.935-26.7731.00 57.30 B O

ATOM5278OE2GLUB 40430.045 -6.264-28.8761.00 56.98 B O

ATOM5279C GLUB 40425.329 -5.724-28.2671,00 50.83 B C

~ 5280O GLUB 40425.479 -4 -28 1 00 49 B O
ATOM~ ~ ~ ~ ~ ~ 632 818 94 I

ATOM5281N TRPB 40524.206 -6.427_ -28.3641.00 50.09 B N
' ATOM5282CA TRPB 40523.092 -5.918-29.1491.00 50.32 B C
i ATOM5283CB TRPB 40521.872 -6.827-29_030__1.0_0_51.22 B C
.

ATOM5284CG TRPB 40520.758 -6.369-29.8991.00 53.25 8 C

ATOM5285CD2TRPB 40519.709 -5.462-29.5401.00 54.19 B C

ATOM5286CE2TRPB 40518.912 -5.266-30.6941.00 54.68 B C
~

ATOM5287CE3TRPB 40519.363 -4.794-28.3561.00 54.45 B C

ATOM5288CD1TRPB 40520.563 -6.678-31.2181.00 54.14 B C

ATOM5289NE1TRPB 40519.456 -6.020-31.7031.00 53.90 B N

ATOM5290CZ2TRPB 40517.784 -4.428-30.6961.00 54.92 B C

ATOM5291CZ3TRPB 40518.240 -3.959-28.3571.00 54.88 B C

ATOM5292CH2TRPB 40517.466 -3.786-29.5221.00 55.10 B C

ATOM5293C TRPB 4D522.712 -4.516-28.6971:00 49.75 B C

ATOM5294O TRPB 40522.399 -3.657-29.5221.00 48.91 B O

ATOM5295N TYRB 40622.733 -4.296-27.3831.00 48.80 B N

ATOM5296CA TYRB 40622.391 -2.993-26.8261.00 48.64 B C

ATOM5297CB TYRB 40622.071 -3.108-25.3251.00 47.74 B C

ATOM5298CG TYRB 40620.586 -3.190-25.0501.00 44.53 B C

ATOM5299CD1TYRB 40619.750 -2.123-25.3551.00 43.21 B C

ATOM5300CE1NR B 40618.373 -2.204-25.1581.00 43.71 B C

ATOM5301CD2TYRB 4062D.011 -4.348-24.5321.00 44.17 B C

ATOM5302CE2TYRB 40618.638 -4.441-24.3291.00 43.95 B C

ATOM5303CZ TYRB 40617.822 -3.362-24.6471.00 44.08 B C

ATOM5304OH TYRB 40616.457 -3.452-24.4741.00 44.59 B O

ATOM5305C TYRB 40623.497 -1.977-27.0491.00 48.71 B C

ATOM5306O TYRB 40623.230 -0.848-27.4451.00 48.02 B O
ATOM5307N GLNB 40724.736 -2.384-26.7941.00 49.19 B N
ATOM5308CA GLNB 40725.874 -1.499-26.9781.00 51.02 B C

ATOM5309CB GLNB 40727.172 -2.244-26.6561.00 51.22 B C

ATOM531DCG GLNB 40728.433 -1.595-27.2221.00 52.71 B C
ATOM5311CD GLNB 40728.769 -0.252-26.5921.00 54.90 B C

ATOM5312OE1GLNB 40729.117 -0.175-25.4111.00 55.65 B O

ATOM5313NE2GLNB 40728.675 0.818 -27.3841.00 55.79 B N

ATOM5314C GLNB 40725.920 -0.948-28.4051.00 52.15 B C
ATOM5315O GLNB 40726.350 0.183 -28.6231.00 52.38 B O

ATOM5316N SERB 40825.467 -1.740-29.3731.00 53.14 B N

ATOM5317CA SERB 40825.472 -1.311-30.7711.00 54.89 B C

ATOM5318CB SERB 40825.356 -2.526-31.7031.00 54.16 B C

ATOM5319OG SERB 40824.054 -3.093-31.6681.00 52.66 B O
ATOM5320C SERB 40824.343 -0.317-31.0751.00 56,38 B C

ATOM5321O SERB 40824.273 0.240 -32.1751.00 56.58 B O
ATOM5322N THRB 40923.469 -0.100-30.0951.00 57.88 8 N

ATOM5323CA THRB 40922.347 0.820 -30.2431.00 59.39 B C

ATOM5324CB THRB 40921.059 0.235 -29.6221.00 59.76 B C
ATOM5325OG1THRB 40920.741 -1.007-30.2611.00 60.15 B O

ATOM5326CG2THRB 40919.892 1.187 -29.8101.00 60.82 B C

ATOM5327C THRB 40922.644 2.168 -29.5881.00 60.24 B C

ATOM5328O THRB 40921.846 3.100 -29.6831.00 60.73 B O

ATOM5329N ILEB 41023.795 2.266 -28.9291.00 61.40 B N

ATOM5330CA ILEB 41024.204 3.504 -28.2691.00 62.56 B C

ATOM5331CB ILEB 41025.299 3.253 -27.2041.00 61.64 B C

ATOM5332CG2ILEB 41025.808 4.579 -26.6521.00 60.28 B C

ATOM5333CG1ILEB 41024.752 2.382 -26.0751.00 60.99 B C

ATOM5334CD1ILEB 41025.811 2.016 -25.0461.00 61.10 B C

ATOM5335C ILEB 41024.785 4.473 -29.2941.00 64.64 B C

ATOM5336O ILEB 41025.884 4.252 -29.8081.00 64.62 B O

ATOM5337N PROB 41124.061 5.566 -29.5931.00 66.38 B N

ATOM5338CD PROB 41122.768 5.951 -29.0041.00 66.82 B C

ATOM5339CA PROB 41124.520 6.571 30.562 1.00 67.95 B C

ATOM5340CB PROB 41123.338 7.533 -30.6441.00 67.52 B C

ATOM5341CG PROB 41122.721 7.432 -29.2821.00 67.83 B C

ATOM5342C PROB 41125.817 7.260 -30.1341.00 69.47 B C

ATOM5343O PROB 41126.333 6.998 -29.0471.00 70.22 B O

ATOM5344N GLNB 41226.336 8.139 -30.9921.00 71.59 B N

ATOM5345CA GLNB 41227.584 8.873 -30.7281.00 73.62 B C

ATOM5346CB GLNB 41227.427 9.840 -29.5441.00 73.73 B C

ATOM5347CG GLNB 41228.707 10.613-29.2431.00 74.25 B C

ATOM5348CD GLNB 41228.546 11.603-28.1091.00 75.31 B C

ATOM5349OE1GLNB 41228.260 11.221-26.9691.00 75.25 B O

ATOM5350NE2GLNB 41228.725 12.887-28.4161.00 75.28 B N

ATOM5351C GLNB 41228.800 7.979 -30.4741.00 74.31 B C

ATOM5352O GLNB 41229.155 7.755 -29.2871.00 74.24 B O

ATOM5353OXTGLNB 41229.385 7.489 -31.4671.00 75.47 B O

ATOM5354CB THRC 860.128 -23.75049.726 1.00 89.25 C C

ATOM5355OG1THRC 86-0.590 -23.16748.630 1.00 89.60 C O

ATOM5356CG2THRC 861.160 -24,72849.182.1.00 89.32 C C

ATOM5357C THRC 86-1.991 -23.51451.011 1.00 88.95 C C
!

ATOM5358O THRC 86-3.016 -23.47250.328 1.00 88.83 C O

ATOM5359N THRC 86-1.395 -25.71550.026 1.00 88.75 C N

ATOM5360CA THRC 86-0.858 -24.47650.661 1.00 88.99 C C
!

ATOM5361N GLUC 87-1.791 -22.74052.075 1.00 88.94 C N

ATOM5362CA GLUC 87-2.780 -21.77452.555 1.00 88.90 C C

ATOM5363CB GLUC 87-2.230 -21.04053.784 1.00 _ C C
90.00 ATOM5364CG GLUC 87-3.108 -19.89154.271 1.00 91.79 C C

ATOM5365CD GLUC 87-2.549 -19.20355.507 1.00 92.73 C C

ATOM5366OEtGLUC 87-2.474 -19.85556.572 1.00 92.76 ~C~
~ ~

ATOM 5367OE2GLUC 87 -2.183 -18.01155.411 1,00 93.11 C O

ATOM 5368C GLUC 87 -3.227 -20.74951.515 1.00 88.00 C C

ATOM 5369O GLUC 87 -4.422 -20.55551.293 1.00 87.56 C O

ATOM 5370N GLNC 88 -2,260 -20.08850.889 1.00 87.38 C N

ATOM 5371CA GLNC 88 -2.543 -19.07049.884 1.00 86.73 C C

ATOM 5372CB GLNC 88 -1.228 -18.51949.335 1,00 86.95 C C

ATOM 5373CG GLNC 88 -1.390 -17.42948.299 1.00 87.10 C C

ATOM 5374CD GLNC 88 -0.071 -16.78047.950 1.00 86.92 C C

ATOM 5375OE1GLNC 88 0.908 -17.46347.643 1.00 86.39 C O

ATOM 5376NE2GLNC 88 -0.034 -15.45347.993 1.00 $6.84 C N

ATOM 5377C GLNC 88 -3.417 -19.58148.738 1.00 86.10 C C

ATOM 5378O GLNC 88 -4.173 -18.81848.138 1.00 85.93 C O

ATOM 5379N GLUC 89 -3,312 -20.87148.439 1.00 85.24 C N

ATOM 5380CA GLUC 89 -4.098 -21.47147.369 1.00 84.32 C C

ATOM 5381CB GLUC 89 -3.400 -22.73346.858 1,00 85.30 C C

ATOM 5382CG GLUC 89 -4.148 -23.45945.755 1.00 86,84 C C

ATOM 5383CD GLUC 89 -3.293 -24.51145.072 1.00 87.89 C C

ATOM 5384OE1GLUC 89 -2.720 -25.37245.776 1.00 88.30 C O

ATOM 5385OE2GLUC 89 -3.19_7-24.47_543.828 1.00 88.15 C O

ATOM 5386C GLUC 89 -5.508 -21.80247.857 1.00 83.07 C C

ATOM 5387O GLUC 89 -6.481 -21.66047.115 1.00 82.93 C O

ATOM 5388N ASPC 90 -5.610 -22.24349.107 1.00 81.52 C N

ATOM 5389CA ASPC 90 -6.901 -22.570.49.703 1.00 79.89.C C
i ATOM 5390CB ASPC 90 -6.709 -23.12451.126 1.00 80.63 C C

ATOM 5391CG ASPC 90 x.584 -24.64151.165 1.00 81.00 C C

ATOM 5392OD1ASPC 90 -6.095 -25.17552.185 1.00 80.78 C O

ATOM 5393OD2ASPC 9D -6.987 -25.30250.186 1.00 81.47 C O

ATOM 5394C ASPC 90 -7.776 -21.32649.758 1.00 78.4$ C C

ATOM 5395O ASPC 90 -8.960 -21.37349.418 1.00 78.01 C O

ATOM 5396N VALC 91 -7.188 -20.21150.188 1.00 76.89 C N

ATOM 5397CA VALC 91 -7.926 -18.95550.291 1.00 75.52 C C

ATOM 5398CB VALC 91 -7.059 -17.83250.898 1.00 75.66 C C

ATOM 5399CG1VALC 91 -7.875 -16.54650.999 1.00 74.96 C C

ATOM 5400CG2VALC 91 -6.550 -18.24952.273 1.00 75.25 C C

ATOM 5401C VALC 91 -8.419 -18.49548.926 1.00 74.48 C C

ATOM 5402O VALC 91 -9.474 -17.8724_8.81$ 1,00 74.33 C O

ATOM 5403N LEUC 92 -7.651 -18.80747.887 1.00 73.03 C N

ATOM 540'4CA LEUC 92 -8.018 -18.42246.531 1.00 71.92 C C

ATOM 5405CB LEUC 92 -6.834 -18,62145.580 1_.00 72.07 C C

ATOM 5408CG LEUC 92 -6.688 -17.61544.432 _1.00 72.15 C C

ATOM 5407CD1LEUC 92 x.547 -18.04943.530 1.00 71.33 C C

ATOM 5408CD2LEUC 92 -7.982 -17.51643.641 1.00 72.35 C C

ATOM 5409C LEUC 92 -9.195 -19.27246.072 1.00 70.75 C C

ATOM 5410O LEUC 92 -10.162-18.75945.512 1.00 70.48 C O

ATOM 5411N ALAC 93 -9.106 -20.57346.319 1.00 69.63 C N

ATOM 5412CA ALAC 93 -10.163-21.49845.940 1_.00 69.26 C C

ATOM 5413CB ALAC 93 -9.743 -22.92246.262 1.00 69.14 C C

ATOM 5414C ALAC 93 -11.478' -21.17046.647 1.00 69.11 C C

ATOM 5415O ALAC 93 -12.551-21.25346.049 1.00 69.74 C O

ATOM 5416N LYSC 94 -11.397-20.79847.919 1.00 68.66 C N

ATOM 5417CA LYSC 94 -12.595-20.46648.683 1.00 68.42 C C

ATOM 5418CB LYSC 94 -12.230-20.19250.152 1.00 69.61 C C

ATOM 5419CG LYSC 94 -13.237-20.72151.186 1.00 70.62 C C

ATOM 5420CD LYSC 94 -13.179-22.24951.303 1.00 71.21 C C

ATOM 5421CE LYSC 94 -14.160-22.79052.347 1.00 71.28 C C

ATOM 5422NZ LYSC 94 -13.855-22.33153.735 1.00 70.41 C N

ATOM 5423C LYSC 94 -13.254-19.22948.062 _1.00 _67.65C C

ATOM 5424O LYSC 94 -14.477-19.17247.913 1.00 67.43 C O

ATOM 5425N GLUC 95 -12.435-18.24447.700 1,00 66.56 C N

ATOM 5426CA GLUC 95 -12.928-17.01447.087 1.0D 65.38 C C

ATOM 5427CB GLUC 95 -11.783-16.00646.928 1.00 65.60 C C

ATOM 5428CG GLUC 95 -11.219-15.4564 8.2351.00 65.24 C C

ATOM 5429CD GLUC 95 -12.238-14.6494 9.0291.00 65.62 C C

ATOM 5430OE1GLUC 95 -13.353-14.4044 8.5121.00 64.$7 C O

ATOM 5431OE2GLUC 95 -11.919-14.25450.172 1.00 65.34 C O

ATOM 5432C GLUC 95 -13.555-17.29445.720 1.00 64.88 C C

ATOM 5433O GLUC 95 -14.597-16.72745.375 1.00 64.01 C O

ATOM 5434N LEUC 96 -12.913-18.17344.952 1.00 64.50 C N

ATOM 5435CA LEUC 96 -13,389-18.54343.621 1.00 65.00 C C
ATOM 5436CB LEUC 96 -12.335-19.39442.908 1.00 64.42 C C

ATOM 5437CG LEUC 96 -11.037-18.68342.515 1.00 64.65 C C

ATOM 5438CD1LEUC 96 -10.029-19.69342.000 1.00 64.28 C C

ATOM 5439CD2LEUC 96 -11.332-17.62741.460 1.00 64.17 C C

ATOM 5440C LEUC 96 -14.71519.30043.650 1.00 65.38 C C

ATOM 5441O LEUC 96 -15.399-19.41242.632 1.00 65.08 C O

ATOM 5442N GLUC 97 -15,069-19.81644.822 1.00 66.02 C N

ATOM 5443CA GLUC 97 -16.304-20.57045.005 1.00 66.89 C C
ATOM 5444CB GLUC 97 -16,332-21.16446.416 1,00 68.67 C C

ATOM 5445CG GLUC 97 -15.356-22.31546.625 1.0D 70.87 C C

ATOM 5446CD GLUC 97 -15.156-22.65948.094 1.00 72.07 C C

ATOM 5447OE1GLUC 97 -16.105-22.45348.885 1.00 72.64 C 0 ATOM 5448OE2GLUC 97 -14.056-23.14548.455 1.00 72.52 C O

ATOM 5449C GLUC 97 -17.565-19.73344.771 1.00 66.09 C C
~

ATOM 5450O GLUC 97 -18.630-20.27044.460 1.00 65.73 C O
ATOM 5451N ASPC 98 -17,442-18.41944.917 1.00 65.13 C N

ATOM 5452CA ASPC 9S -18.578-17:52644.724 1.00 64.11 C C

ATOM5453CB ASPC 98 -18.524-16.39445.752 1.00 65.46 C C

ATOM5454CG ASPC 98 -18.597-16.90447,181 1.00 66.99 C C

ATOM5455OD1ASPC 98 -19.582-17.603_ 1.00 67.75 C O
_47.513 ATOM5456OD2ASPC 98 -17.671-16.60947.9_68 1,00 _6_7.81C O

ATOM5457C ASPC 98 -18.619-16.94943.310 1.00 62.83 C C

ATOM5458O ASPC 98 -19.248-15.91643.064 1.9D 62.13 C O

ATOM5459N VALC 99 -17.956-17,63642.384 1.00 60.78 C N
ATOM5460CA VALC 99 -17,892-1720940.991 1,00 58.84 C C

ATOM5461CB VALC 99 -17.103-18.22840.138 1.00 59.34 C C

ATOM5462CG1VALC 99 -17.830-19.56240.114 1.00 58.83 C C

ATOM5463CG2VALC 99 -18.917-17.69338,728 1.00 59.37 C C

ATOM5464C VALC 99 -19.261-16.99840.351 1.00 57.28 C C

ATOM5465O VALC 99 -19.420-16.12939.499 1.00 56.28 C O
ATOM5466N ASNC 100-20.246-17.79240.757 1.00 56,45 C N

ATOM5467CA ASNC 100-21.590-17.67140.201 1.00 55.04 C C

ATOM5468CB ASNC 100-22.259-19.04740.106 1.00 55.59 C C

ATOM5469CG ASNC 100-21,424-20.05639:320 1.00 56.23 C C

ATOM5470OD1ASNC 100-20.542-19.68338.549 1.00 55.83 C O

ATOM5471ND2ASNC 100-21.715-21.34139.505 1.00 56.14 C N

ATOM5472C ASNC 100-22.441-16,73741.047 1.00 54.36 C C

ATOM5473O ASNC 100-23.660-16.66540.883 1.00 53.98 C O

ATOM5474N LYSC 101-21.787-16.01441.949 1.00 53.88 C N

ATOM5475CA LYSC 101-22.486-15.07942.820 1.00 53.43 C C

ATOM5476CB LYSC 101-22.061-15.26444.281 1.00 54.86 C C

ATOM5477CG LYSC 101-22.550-16.52244.986 1.0D 56.59 C C

ATOM5478CD LYSC 101-22.130-16.45346.458 1.00 57.86 C C
' ATOM5479GE LYSC 101-22.661-17.61147.293 1.00 59.18 C C

ATOM5480NZ LYSC 1p1-22.418-17.37348.756 1.00 59.33 C N

ATOM5481C LYSC 101-22:221-13.63042,443 1.00 52.51 C C

ATOM5482O LYSG 101-21.104-13.25842.085 1.00 51.82 C O

ATOM5483N TRPC 102-23.259-12.81242.539 1.D0 51.31 C N

ATOM5484CA TRPC 102-23,127-11.39842.257 1.00 51.04 C C

ATOM5485CB TRPC 102-24.501-10.77142.014 1.00 51.95 C C

ATOM5486CG TRPC 102-24.450-9.36541.491 1.00 52.92 C C

ATOM5487CD2TRPC 102-24,341-8,96840.119 1.00 52.91 C C

ATOM5488CE2TRPC 102-24.365-7.55340.088 1.00 53.62 C C

ATOM5489CE3TRPC 102-24.229-9.87038.911 1.00 53.02 C C

ATOM5490CD1TRPC 102-24.524-8.21042,218 1,00 53,83 C C

ATOM5491NE1TRPC 102-24.477-7.11541.382 1.00 53.05 C N

ATOM5492C22TRPC 102-24.283-6.82738.894 1.00 53.16 C C
ATOM5493CZ3TRPC 102-24.147-8.94737.722 1.00 52.57 C C

ATOM5494CH2TRPC 102-24.176-7.53937.726 1.00 53.05 C C
.

ATOM5495C TRPC 102-22.503-10.80643.505 1.00 50.38 C C

ATOM5496O TRPC 102-23.148-10.71944.546 1.00 51.04 C O

ATOM5497N GLYC 103-21.239-10.42043.416 1.00 49.78 C N

ATOM5498CA GLYC 103-20.595-9.84944.580 1.00 48.53 C C
ATOM5499C GLYC 103-19.259-10,50244.835 1.00 48.48 C C

ATOM5500O GLYC 103-18.695-10.36945.920 1.00 46.87 C O
ATOM5501N LEUC 104-18.753-11.21143.831 1.00 48.94 C N
ATOM5502CA LEUC 104-17.462-11.87243.947 1.00 49.79 C C

ATOM5503CB LEUC 104-17.024-12.42242.587 1.00 49.93 C C
ATOM5504CG LEUC 104-15.619-13.03242.534 1.00 50.83 C C

ATOM5505CD1LEUC 104-15.455-14,04843.6 471.00 51.77 C C

ATOM5506CD2LEUC 104-15.394-13.68841,1 851.00 50.75 C C
ATOM5507C LEUC 104-16.418-10.88844.4 681.00 49.87 C C
ATOM5508O LEUC 104-16,427-9.71544.1 061.00 50,43 C O

ATOM5509N HISC 105-15.531-11,36945.329 1.00 49.82 C N
ATOM5510CA HISC 105-14,480-10.53345.892 1.00 50.37 C C

ATOM5511CB HISC 105-13.985-11.15047.206 1.00 52.02 C C

ATOM5512CG HISC 105-15,050-11.28848,252 1,00 54.02 C C

ATOM5513CD2HISC 105-16.325-10.82848.296 1.00 54.60 C C
ATOM5514ND1HISC 105-14,841-11,94849,445 1,00 55.3D C N

ATOM5515CE1HISC 105-15.940-11,88750.179 1.00 55.19 C C
ATOM5516NE2HISC 105-16.855-11.21349.505 1.00 54.74 C N
ATOM5517C HISC 105-13.346-10.46844.868 1,00 49.74 C C

ATOM5518O HISC 105-12.210-10.87945.141 1.00 48.89 C O

ATOM5519N VALC 106-13.669-9.94443.687 1.00 49.23 C N
ATOM5520CA VALC 106-12.711-9.84842.588 1.00 48,37 C C

ATOM5521CB VALC 106-13.340-9.13441.358 1.00 48.77 C C
ATOM5522CG1VALC 106-13.715-7.70041.707 1.00 48.47 C C

ATOM5523CG2VALC 106-12.374-9.17640.184 1,00 47,49 C C

ATOM5524C VALC 106-11.378-9.19842.941 1.00 47.81 C C
ATOM5525O VALC 106-10.335-9.63342.458 1.00 47.97 C O
ATOM5526N PHEC 107-11,398-8.16843.781 1.00 47.98 C N

ATOM5527CA PHEC 107-10,155-7,50644.182 1.00 48.26 C C
ATOM5528CB PHEC 107-10.459-6.21444.952 1.00 48.60 C C
ATOM5529CG PHEC 107-11.000-5.10744.088 1.00 49.76 C C

ATOM5530CD1PHEC 107-10.181x.467 43,160 1,00 W.15 C C
ATOM5531CD2PHEC 107-12.332-4.71744.186 1.00 50.03 C C
ATOM5532CE1PHEC 107-1D.680-3,45242.338 1.00 50.69 C C

ATOM5533CE2PHEC 107-12.8483.703 43.370 1.00 51.00 C C
ATOM5534CZ PHEC 107-12.019-3,06942.443 1.00 51.67 C C
ATOM5535C PHEC 107-9.308 -8.44345.045 1.00 48.82 C C

ATOM5536O PHEC 107-8.080 -8.50244,906 1.00 47.92 C O
-ATOM5537N ARGC 108-9.972 -9.17445.938 1.00 49.29 C N
ATOM5538CA ARGC 108-9.290 -10.11946.818 1.00 49.89 C C

ATOM 5539CB ARGC 108-10.304-10.84047.722 1.00 51.44 C C

ATOM 5540CG ARGC 108-9.846 -11.07949.162 1.00 52.57 C C

ATOM 5541CD ARGC 108-8.473 -11.70849.241 1.00 53.85 C C

ATOM 5542NE ARGC 108-7.948 -11.65150.602 1.00 54.93 C N

ATOM 5543CZ ARGC 108-6.654 -11.57750.901 1.00 54.84 C C

ATOM 5544NH1ARGC 108-5.744 -11.55149.937 1.00 53.43 C N

ATOM 5545NH2ARGC 108x.269 -11.52452:168 1.00 55.22 C N

ATOM 5546C ARGC 108-8.614 -11.14745.920 1.00 49.48 C C

ATOM 5547O ARGC 108-7.451 -11.50346.112 1.00 49.27 C O

ATOM 5548N ILEC 109-9.365 -11.61544.930 1.00 48.52 C N

ATOM 5549CA ILEC 109-8.865 -12.61244.002 1.00 48.80 C C

ATOM 5550CB ILEC 109-9.969 -13.04243.011 1.00 47.92 C C

ATOM 5551CG2ILEC 109-9.375 -13.89241.905 1.00 45:85 C C

ATOM 5552CG1ILEC 109-11.066-13.79043.777 1.00 46.57 C C

ATOM 5553CDiILEC 109-12.205-14.29942.926 1.00 47.45 C C

ATOM 5554C ILEC 109-7.636 -12.15143.232 1.00 48.

ATOM 5555O ILEC 109-6.714 -12.93543.025 1.00 50.48 C O

ATOM 5556N ALAC 910-7.613 -10.88942.817 1.00 48.05 C N

ATOM 5557CA ALAC 110$.466 -10.36342.081 1.00 48.48 C C

ATOM 5558CB ALAC 110-6.735 -8.92841.630 1.00 47,16 C C

ATOM 5559C ALAC 110x.218 -10.41142.956 1.00 49,00 C C

ATOM 5560O ALAC 110-4,142 -10.78242.491 1.00 48.96 C O

ATOM 5561N GLUC 111-5.369 -10.04244.225 1.00 49.68 C N

ATOM 5562CA GLUC 111-4.249 -10.04645.163 1.00 51.20 C C
~

ATOM 5563CB GLUC 111-4.694 -9.52246.544 1.00 52.69 C C

ATOM 5564CG GLUC 111-5.095 -8.04046.608 1.0D 55.69 C C
~

ATOM 5565CD GLUC 111-5.625 -7.62047.988 1.00 57.11 C C
' ATOM 5566OE1GLUC 111-6,583 -8.25448.480 1.00 57.71 C O

ATOM 5567OE2GLUC 111-5.095 -6.65248.580 1.00 57.55 C O

ATOM 5568C GLUC 111-3.649 -11.44645.339 1.00 51.12 C C

ATOM 5569O GLUC 111-2.431 -11.61345.373 1.00 50.42 C O

ATOM 5570N LEUC 112-4.517 -12.44845.437 1.00 52.01 C N

ATOM 5571CA LEUC 112-4.098 -13.82845.663 1.00 52.02 C C

ATOM 5572CB LEUC 112-5.244 -14.59746.328 1.00 .

ATOM 5573CG LEUC 112-5.699 -13.98447.658 1.00 52.22 C C

ATOM 5574CD1LEUC 112-6.934 -14.69548.191 1.00 50.89 C C

ATOM 5575CD2LEUC 112-4.545 -14.48348.657 1.00 53.16 C C

ATOM 5576C LEUC 112-3.583 -14.61644.4_581.00 52.32 C C

ATOM 5577O LEUC 112-2.899 -15.627_44.6341.00 52.65 C O

ATOM 5578N SERC 113-3.899 -14.17343.244 1.00 51.67 C N

ATOM 5579CA SERC 113-3.437 -14.88742.051 1.00 51.10 C C

ATOM 5580CB SERC 113-4.573 -15.00241,022 1.00 50.69 C C

ATOM 5581OG SERC 113-5.061 -13.72740.646 1.04 49.84 C O

ATOM 5582C SERC 113-2.218 -14.22241.405 1.D0 50.61 C C

ATOM 5583O SERC 113-1.909 -14.48440.243 9.00 50.67 C O

ATOM 5584N GLYC 114-1.526 -13.37242.162 1.00 50.38 C N

ATOM 5585CA GLYC 114-0.355 -12.690__41.63_59.00 50.55 C C

ATOM 5586C GLYC 114-0.734 -11.69640.551 1.00 50.91 C C

ATOM 5587O GLYC 1140.019 -11.45439.604 1.00 50.92 C O

ATOM 5588N ASNC 115-1.922 -11.12340.708 1.00 50.77 C N

ATOM 5589CA ASNC 115-2.484 -10.15639.775 1.00 49.31 C C

ATOM 5590CB ASNC 115-1.510 -9.00139.529 1.00 SD.12 C C

ATOM 5591CG ASNC 115-2.144 -7.86238.735 1.00 51.70 C C

ATOM 5592OD1ASNC 115-0.179 -7.31239._1_241.00 52.40 C O

ATOM 5593ND2ASNC 115-1.521 -7.50337.619 1.00 52.28 C N

ATOM 5594C ASNC 115-2.890 -10.79538.451 1.00 48.23 C C

ATOM 5595O ASNC 115~ -2.620-10.25737.380 1.00 48.82 C O

ATOM 5596N ARGC 116-3.529 -11.95638.525 1.0D 47.11 C N

ATOM 5597CA ARGC 116-4.018 -12.62937.323 1.00 46.74 C C

ATOM 5598CB ARGC 1163.219 -13.90437.015 1.00 48.26 C C

ATOM 5599CG ARGC 116-1.957 -13.67D36.179 1.00 50.94 C C

ATOM 5600CD ARGC 116-1.862 -14.66035.019 1.00 52.40 C C

ATOM 5601NE ARGC 116-0.643 -14.481_ 34.2331.00 54.63 C N

ATOM 5602CZ ARGC 116-0.312 -13.35433.602 1.0D 55.61 C C

ATOM 5603NHiARGC 116-1.108 -12.29733.659 1.00 56.84 C N

ATOM 5604NH2ARGC 1160.821 -13.28032.916 1.00 55.14 C N

ATOM 5645C ARGC 116-5.489 -12.97831.487 1.00 44.59 G C

ATOM 5606O ARGC 116-5.915 -14.08137.160 1.00 44.52 C O

ATOM 5607N PROC 117-6.290 -12.02737.985 1.00 43.62 C N

ATOM 5608CD PROG 117-5.967 -10.61738.262 1.D0 43.61 C C

ATOM 56D9CA PROC 117-7.720 -12.26938.184 1.00 43.51 C C

ATOM 5610CB PROC 117x.212 -10.94538.782 1.00 42.38 C C

ATOM 5611CG PROC 117-7.326 -9.94 8 38.1511.00 42.72 C C

ATOM 5612C PROC 117-8.469 -12.65936.910 1.00 42.83 C C

ATOM 5613O PROC 117-0.301 -13.56536.931 9.00 43.55 C O

ATOM 5614N LEUC 118-8.172 -11.98135.8D6 1.00 41.88 C N

ATOM 5615CA LEUC 118-8.834 -12.27134.540 1.00 41.56 C C

ATOM 5616CB lEUC 118-8.382 -11.28733.444 1.00 39.34 C C

ATOM 5617CG LEUC 118-8.974 -11.53132.048 1.00 37.19 C C

ATOM 5618CD1LEUC 118-10.483-11.66332.131 1.00 36.26 C C

ATOM 5619CD2LEUC 118-8.586 -10.39431.114 1.00 38.92 C C

ATOM 5620C LEUC 118-8,544 -13.70234.097 1.00 42.16 C C

ATOM 5621O LEUC 118-9.424 -14.39833.586 1.00 41.78 C O

ATOM 5622N THRC 119-7.309 -14.14234.288 1.00 42.99 C N

ATOM 5623CA THRC 119-6.954 -15.49333.900 1.00 44.32 C C

ATOM 5624CB THRC 119-5.437 -15.73234.018 1.00 44.98 C C

ATOM5625OG1THRC 119-4.750 -14.961 33.0251.00 44.76 C O

ATOM5626CG2THRC 1195.112 -17.210 33.8281.00 45.52 C C

ATOM5627C THRC 119-7.689 -16.522 34.7541.00 44.75 C C

ATOM5628O THRC 119-8.371 -17.396 34.2231.00 44.05 C O

ATOM5629N VALC 120-7.563 -16.411 36.0741.00 45.34 C N

ATOM5630CA VALC 120-8.213 -17.363 38.9731.00 45.59 C C

ATOM5631CB VALC 120-7.842 -17.101 38.4591.00 45.97 C C

ATOM5632CG1VALC 120-6,328 -17.183 38,6401.00 46,71 C C

ATOM5633CG2VALC 120-8.367 -15.754 38.9081.00 46.08 C C

ATOM5634C VALC 120-9.735 -17.364 36.8291.00 45.62 C C

ATOM5635O VALC 120-10.340-18.424 36.6471.00 45.97 C O

ATOM5636N ILEC 121-10.350-16.187 36.8891.00 45.48 C N

ATOM5637CA ILEC 121-11.799-16.089 36.7621.00 45.38 C C

ATOM5638CB ILEC 121-12,277-14.620 36.9511,00 44.53 C C

ATOM5639CG2ILEC 121-13.760-14.487 36.6071.00 44.47 C C

ATOM5640CG1ILEC 121-12.031-14.183 38.4031.00 44.74 C C

ATOM5641CD1ILEC 121-12.520-12.782 38.7431.00 41.83 C C

ATOM5642C ILEC 121-12.286-16.641 35.4211.00 46.24 C C

ATOM5643O iLEC 121-13.264-17,386 35.3751.00 46,14 C O

ATOM5644N METC 122-11.605-16.291 34:3331.00 47.70 C N

ATOM5645CA METC 122-11.996-16.778 33.00$1.00 48.56 C C

ATOM5646CB METC 122-11.157-16.108 31.9091.00 49,54 C C

ATOM5847CG METC 122-11.692-14.768 31:4011.00 49.77 C C

ATOM5648SD METI 122-13.106-14.954 30:2991.00 48.84 C S
C

ATOM5649CE METC 122-12.256-15.494 28.8151.00 48.42 C C

ATOM5650C METv 122-11.850-18.293 32.890_ 49.11 C C
C 1.00 ATOM5651O MET' 122-12.689-18.961 32.2911.00 46.51 C O
C

ATOM5652N HISC 123-10.776-18.835 33:4531.00 51.31 C N

ATOM5653CA HISC 123-10.558-20.273 33.3801.00 53.67 C C

ATOM5654CB HISC 123-9.126 -20.640 33.7931.00 55.59 C C

ATOM5655CG HiSC 123$.799 -22.088 33.5821,00 58.32 C C

ATOM5656CD2HISC 123-8.283 -23.021 34,4181.00 59.53 C C

ATOM5657ND7HISC 123-9.034 -22.735 32.3881.00 59.09 C N

ATOM5658CE1HISC 123-8.680 -24.003 32.4971.00 59.40 C C

ATOM5659NE2HISC 123-8.222 -24.203 33.7201.00 59.91 C N

ATOM5660C HISC 123-11.559-21.001 34.2691.00 53.28 C C

ATOM5661O HISC 123-12.050-22.069 33.9101,00 52.59 C O

ATOM5662N THRC 124-11.858-20.412 35,4241,00 53,28 C N

ATOM5663CA THRC 124-12.818-20.992 36.3571.00 53.19 C C

ATOM5664CB THRC 124-12.874-20.194 37.6791.00 53.87 C C

ATOM5665OG1THRC 124-11.632-20.340 3$.3841.00 54.25 C O

ATOM5666CG2THRC 124-14.012-20.693 38.5581.00 54.46 C C

ATOM5667C THRC 124-14.203-20.987 35.7231.00 52.92 C C

ATOM5668O THRC 124-14.897-21.996 35.7271.00 53.15 C O

ATOM5669N ILEC 125-14.600-19.844 35:1741.00 53.29 C N

ATOM5670CA ILEC 125-15.904-19.712 34.5291.00 53.63 C C

ATOM5671CB ILEC 125-16.155-18.244 34.0931.00 53.05 C C

ATOM5672CG2ILEC 125-17.301-18.166 33.0921.00 51.98 C C

ATOM5673CG1ILEC 125-16,452-17.395 35.3351,00 52.45 C C

ATOM5674CD1ILEC 125-16.453-15.907 35.0921.00 52.11 C C

ATOM5675C ILEC 125-16.026-20.640 33.3241.00 54.11 C C

ATOM5676O ILEC 125-17.127-21.073 32.9781.00 54.36 C O

ATOM5677N PHEC 126-14.893-20.952. 32.6981.00 54.49 C N

ATOM5678CA PHEC 126-14.871-21.834 31.5321.00 54.69 C C

ATOM5679CB PHEC 126-13.559-21.657 30 1.00 54.33 C C
.760 ATOM5680CG PHEC 126-13.673-20,743 _ 1.00 53.71 C C
29.570 ATOM5681CDtPHEC 126-14.207-19,462 29.7041.00 53.94 C C

ATOM5682CD2PHEC 126-13.273-21.172 28.3091.00 52.91 C C

ATOM5683CE1PHEC 126-14.343-18.628 28.5931.00 53.57 C C

ATOM5684CE2PHEC 126-13.407-20.346 27.1971.00 52.45 C C

ATOM5685CZ PHEC 126-13.944-19.07427.3401.00 52,37 C C
ATOM5686C PHEC 126-15.074-23.31231.8771.00 55.33 C C

ATOM5687O PHEC 126-15.505-24.09731,0341.00 55.31 C O

ATOM5688N GLNC 127-14.756-23.69733.1071.00 56.08 C N

ATOM5689CA GLNC 127-14.943-25.082 33.5251.00 57.16 C C

ATOM5690CB GLNC 127-13.933-25.461 34.6071.00 58.57 C C
ATOM5691CG GLNC 127-12.504-25.251 34.1911.00 _59.73C C

ATOM5692CD GLNC 127-11.549-25.419 35.3391.00 61.99 C C

ATOM5693OE1GLNC 127-11.774-24,890 36,4361.00 62.22 C O

ATOM5694NE2GLNC 127-10.463-26.149 35.0981.00 62.86 C N

ATOM5695C GLNC 127-16.360-25.213 34.0691.00 57.04 C C

ATOM56960 GLNC 127-17.033-26.212 33.8301.00 57.87 C O

ATOM5697N GLUC 128-16.805-24.195 34.8021,00 56.68 C N

ATOM5698CA GLUC 128-18.154-24.183 35.3631,00 56.61 C C
ATOM5699CB GLUC 128-18.376-22.900 36.1731,00 56.24 C C
ATOM5700CG GLUC 1_28-19.834-22.485 36:3881.00 57.69 C C

ATOM5701CD GLUC __128-20.667-23,493 37.1551.00 59.61 C C

ATOM5702OE1GLUC 128-20.193-23.989 38.2051.00 58.33 C O

ATOM57030E2GLUC 128-21.811-23.773 36.7261.00 60.32 C O

ATOM5704C GLUC 128-19,170-24,276 34.2261.00 56,21 C C

ATOM5705O GLUC 128-20.305-24,702 34.4271,00 55.69 C O
ATOM5706N ARGC 129-18.746-23.885 33.0281.00 55.92 C N

ATOM5707CA ARGC 129-19.616-23:931 31 1.00 55.72 C C
.860 ATOM5708CB ARGC 129-19.660-22.558 _ 1.00 55.68 C C
31.190 ATOM5709CG ARGC 129-20,536-21.593 31.9481,00 55.36 C C

L 5710CD ARGC 129-20.445-20.181 31 1 00 55 C C
ATOMI I I I I ~ ~ 427 84 I

ATOM5711NE ARGC 129-21.419-19.33532.1091.00 55.44 C N
ATOM5712CZ ARGC 129-22.735-19.46231_.9731.00 54.00 C C
ATOM5713NH1ARGC 129-23.228-20.39731.1721.00 54.29 C N

ATOM5714NH2ARGC 129-23.554-18.66332.6411.00 53.39 C N

ATOM5715C ARGC 129-19.1 -25.00130.8681.00 55.36 C C
ATOM5716O ARGC 129SR -25.08329.7591.00 54.44 C O
ATOM5717N ASPC 130-19.714-25.82131.2871.00 55.21 C N
-18.221 ATOM5718CA ASPC 130-17.705-26.91730.4691.00 56.06 C C

ATOM5719CB ASPC 130-18.709-28.08330.4801.00 56.73 G C
ATOM5720CG ASPC 130-18.079-29.41230.0831.00 57.26 C C
ATOM5721OD1ASPC 130-17.141-29.86230.7771.00 55.78 C O
ATOM5722OD2ASPC 130-18.52630.00929.0781.00 58.74 C O

ATOM5723C ASPC 130-17,427-26.47829.0301.00 56.10 C C

ATOM5724O ASPC 130-17.514-27.27928.0991.00 56.16 C O
ATOM5725N LEUC 131-17.084-25.20328.8551.00 56.40 C N
ATOM5726CA LEUC 131-16.794-24.65027.5311.00 56.01 C C

ATOM5727CB LEUC 131-16,623-23.13427.6321.00 55.54 C C

ATOM5728CG LEUC 131-17.861-22.35028.0831.00 54.99 C C
ATOM5729CD1LEUC 131-17.462-20.91528.4321.00 53.56 C C

ATOM5730CD2LEUC 131-18.916-22.37326.9811.00 53.77 G C

ATOM5731C LEUC 131-15.563-25.27526:8611.00 55.70 C C

ATOM5732O LEUC 131-15.567-25.51925.6581.00 55.55 C O

ATOM5733N LEUC 132-14.509-25.53027.6271.00 56.78 C N

ATOM5734CA LEUC 132-13.311-26.13927.0501.00 57.99 C C
ATOM5735CB LEUC 132-12.273-26.46428.1341.00 57.70 C C

ATOM5736CG LEUC 132-11.667-25.32428.9591.00 58.20 C C

ATOM5737CD1LEUC 132-12.550-25.01930.1561.00 57.08 C C

ATOM5738CD2LEUC 132-10.281-25.73229.4361.00 57.96 C C
ATOM5739C LEUC 132-13.687-27.42326.3041.00 58.47 C C

ATOM5740O LEUC 132-13.156-27.70525.2261.00 57.96 C O

ATOM5741N LYSC 133-14.611-28.19126.8811.00 59.44 C N

ATOM5742CA LYSC 133-15.068-29.44026.2751.00 59.54 C C

ATOM5743CB LYSC 133-15.703X0.34727.3341.00 60.73 C C

ATOM5744CG LYSC 133-16.20931.67326.7851.00 61.68 C C

ATOM5745CD LYSC 133-16.877-32.50127.8651.00 62.98 C C

ATOM5746CE LYSC 133-17.501-33.76027.2881.00 63.42 C C

ATOM5747NZ LYSC 133-18.259-34.51528.3251.00 64.63 C N

ATOM5748C LYSC 133-16.063-29.21925.1311.00 58.74 C C

ATOM5749O LYSC 133-15.982-29.88624.0991.00 59.75 C O
ATOM5750N THRC 134-16.999-28.29025.3021.00 57.11 C N

ATOM5751CA THRC 134-17.976-28.03524.2471.00 56.71 C C
ATOM5752CB THRC 134-18,983-26.93424.6371.00 56.23 C C

ATOM5753OG1THRC 134-19,586-27.24925.8961.00 57.09 C O

ATOM5754CG2THRC 134-20,065-26.81723.5851.00 55.09 C C
ATOM5755C THRC 134-17.303-27.58422.9541.00 57.04 C C
ATOM5756O THRC 134-17.813-27.83621.8621.00 56.62 C O

ATOM5757N PHEC 135-16.159-26.91623.0751.00 56.75 C N

ATOM5758CA PHEC 135-15.460-26.41521.8951.00 56.98 C C

ATOM5759CB PHEC 135-15.418-24.88121.9481.00 55.53 C C
ATOM5760CG PHEC 135-16.786-24.22521.9341.00 53.72 C C

ATOM5761CDtPHEC 135-17.565-24.22220.7791.00 52.24 C C

ATOM5762CD2PHEC 135-17.288-23.60223.0761.00 53.57 C C
ATOM5763CE1PHEC 135-18.822-23.60620.7551.00 51.74 C C

ATOM5764CE2PHEC 135-18.553-22.98023.0631.00 52.82 C C
ATOM5765CZ PHEC 135-19.318-22.98521.8971.00 51.42 C C

ATOM5766C PHEC 135-14.049-26.97921.7231.00 57.53 C C

ATOM5767O PHEC 135-13.249-26.44920.9591.00 56.93 C O

ATOM5768N LYSC 136-13.756-28.06822.4241.00 59.33 C N

ATOM5769CA LYSC 136-12,438-28.70122.3561.00 60.85 C C

ATOM5770CB LYSC 136-12.282,29.48621.0471.00 62.49 C C

ATOM5771CG LYSC 136-13.278-30.62020.8351.00 64.02 C C

ATOM5772CD LYSC 136-13.074-31.25619.4591.00 65.06 C C
ATOM5773CE LYSC 136-14.103-32.34319.1791.00 66.50 C C

ATOM5774NZ LYSC 136-14.036X3.44220.1881.00 66.51 C N

ATOM5775C LYSC 136-11.316-27.66522.4461.00 60.83 C C

ATOM5776O LYSC 136-10.552-27.49021.4981.00 61.68 C O

ATOM5777N ILEC 137-11.219-26.97923.5801.00 60.03 C N

ATOM5778CA ILEC 137-10.180-25.97223.7661.00 59.10 C C

ATOM5779CB ILEC 137-10.725-24.71924.4791,00 59.17 C C

ATOM5780CG2ILEC 137-9.615 -23.68324.6111.00 59.41 C C

ATOM5781CG1ILEC 137-11.915-24.14323.7051.00 58.59 C C

ATOM5782CD1ILEC 137-12.539-22.93524.3661.0O 56.94 C C

ATOM5783C ILEC 137-9,023 -26.51424.5981.00 58.66 C C

ATOM5784O ILEC 137-9.153 -26.71325.8051.00 57.69 C O

ATOM5785N PROC 138-7.871 -26.76123.9611.00 58.62 C N

ATOM5786CD PROC 138-7.534 -26.56822.5431.00 58.83 C C

ATOM5787CA PROC 138-6.726 -27.27824.7121.00 58.90 C C

ATOM5788CS PROC 138-5.605 -27.31623.6691.00 58.68 C C

ATOM5789CG PROC 138-6.057 -26:34522.6121.00 59.32 C C

ATOM5790C PROC 138-6.390 -26.42225.9321.00 59.34 C C

ATOM5791O PROC 138x,287 -25.20025.8471.00 _ C O
59.12 ATOM5792N VALC 139-6.237 -27.09227.0691.00 59.50 C N

ATOM5793CA VALC 139-5.932 -26.44628,3381.00 59.96 C C

ATOM5794CB VALC 139-5.577 -27.50929.4181.00 59.15 C C

ATOM5795CG1VALC 139-6.620 -28.59929.4121,00 59.39 C C

ATOM5796CG2VALC 139x.206 -28.11329.1611,00 58.88 C C

ATOM 5797C VALC 139-4_.805-25.41728.257 1.00 ~ 60.22C C

ATOM 5798O VALC 139-4.949 -24.29128.739 1,00 59.81 C O

ATOM 5799N ASPC 140-3.693 -25.80627.641 1.00 60.79 C N

ATOM 5800CA ASPC _ -2.531 -24.93527.515 1.00 61.38 C C

ATOM 5801GB ASPC 140-1.337 -25.72526.967 1.00 62.69 C C

ATOM 5802CG ASPC 140-1.628 -26.37225.621 1.00 64.23 C C

ATOM 5803OD1ASPC 140-0.668 -26.83024.961 1.00 64.36 C O

ATOM 58x4OD2ASPC 140-2.814 -26.42925.224 1.00 65.38 C O

ATOM 5805C ASPC 140-2.790 -23.72026.635 1.00 61.19 C C

ATOM 5806O ASPC 140-2.273 -22.63526.899 1.00 61.82 C O

ATOM 5807N THRC 1413.588 -23.89825.588 1.00 60.26 C N

ATOM 5808CA THRC 141-3.892 -22.79624.688 1.00 58.97 C C

ATOM 5809CB THRC 141X1.746 -23.26523.459 1.0D 58.71 C C

ATOM 5810OG1THRC 141-4.009 -24.22922:726 1.00 58.33 C O

ATOM 5811CG2THRC 141-5.102 -22.08522.593 1.00 57.58 C C

ATOM 5812C THRC 141-4.646 -21.70925.437 1.00 58.36 C C
' ATOM 5813O THRC 141-4.220 -20.55425.468 1.00 58.97 C O

ATOM 5814N LEUC 1425.763 -22.09226.047 1.00 57.24 C N
!

ATOM 5515CA LEUC 142-8.590 -21.15726.795 1.00 55.44 C C
' ATOM 5816CB LEUC 142-7.705 -21.90627.519 9.00 55.66 C C

ATOM 5817CG LEUC 142-8.598 -21.02828.398 1.00 55.74 C C

ATOM 5818CDtLEUC 142-9.356 -20.03527.520 1,00 55.71 C C

ATOM 5819CD2LEUC 142-9.559 -21.90229.196 1.00 55.52 C C

ATOM 5820C LEUC 142-5.776 -20.35727.807 1.00 54.02 C C

ATOM 5821O LEUC 142-5,854 -19.13127.845 1.00 53.26 C O

ATOM 5822N ILEC 143-4.899 -21.04728.633 1.00 52.78 C N

ATOM 5823CA ILEC 143-4.198 -20.34629.621 1.00 52.83 C C

ATOM 5824CB ILEC 143-3.373 -21.30930.493 1.00 52.56 C C

ATOM 5825CG2ILEC 143-2.673 -20.52831.592 1.00 52.10 C C

ATOM 5826CG1ILEC 143-4.290 -22.34831.136 1.00 53.74 C C

ATOM 5827CD1ILEC 143-3.60_5-23.21132.188 1.00 54.46 C C

ATOM 5828C ILEC 143-3.257 -19.36528.917 1.00 52.77 C C

ATOM 5829O ILEC 143-3.195 -18.18629.284 1.00 52.59 C O

ATOM 5830N THRC 144-2.546 -19.84427.896 1.00 51.30 C N

ATOM 5831CA THRC 144-1.625 -18.98327.161 1.00 50.35 C C

ATOM 5832CB THRC 144-0.900 -19.74326.014 1.00 50.77 C C

ATOM 5833OG1THRC 1440.046 -20.66726.572 1.00 51.37 C O

ATOM 5834CG2THRC 144-0.147 -18.76825.123 1.00 49.84 C C

ATOM 5835C THRC 144-2.328 -17.74626.593 1.00 48.34 C C

ATOM 5836O THRC 144-1.798 -16.64026.694 1.00 48.98 C O

ATOM 5837N TYRC 145-3.510 -17.92026.007 1.00 45.47 C N

ATOM 5838CA TYRC 145-4.225 -16.77525.469 1.00 43.03 C C

ATOM 5539CB TYRC 1455.499 -17.18924.744 1.00 42.09 C C

ATOM 5840CG TYRC 145-6.327 -15.99324.319 1.00 40.97 C C

ATOM 5841CD1TYRC 145-6.004 -15.27423.166 1.00 40.19 C C

ATOM 5842CEtTYRC 145-6.730 -14.13722.790 1,00 40.74 C C

ATOM 5843CD2TYRC 945-7.400 -15.54825.093 1.00 39.98 C C

ATOM 5844CE2TYRC 145-8.137 -14.40124.728 1.00 39.71 C C

ATOM 5845CZ TYRC 145-7.792 -13.70523.576 1.00 39.55 C C

ATOM 5846OH TYRC 145-8.481 -12.57223.212 1.00 39.59 C O

ATOM 5847C TYRC 145-4.624 -15.83526.597 1.00 43.67 C C

ATOM 5848O TYRC 145-4.351 -14.63326.539 1,00 43.90 C O

ATOM 5849N LEUC 146-5.285 -16.38927.612 1.00 42.64 C N

ATOM 5850CA LEUC 146-5.746 -15.60528.750 1.00 43.14 C C

ATOM 5851CB LEUC 146-6.415 -16.52329.788 1.00 43.11 C C

ATOM 5852CG LEUC 146-7.721 -17.22029.360 1.00 42.51 C C

ATOM 5853CD1LEUC 146-8.232 -18.13030.489 1.00 41.92 C C

ATOM 5854CD2LEUC 146-8.771 -16.16728.987 1.00 41.24 C C

ATOM 5855C LEUC 146-4.614 -14.80029.396 1,00 43.64 C C

ATOM 5856O LEUC 146x.804 -13.64229.775 1.00 42.97 C O

ATOM 5857N METC 147-3.437 -15.40629.515 1.00 44.18 C N

ATOM 5858CA METC 147-2.300 -14.71130.105 1.00 44.81 C C

ATOM 5859CB METC 147-1.106 -15.64830.264 1.00 47.04 C C

ATOM 5860CG METC _ -1.369 -16.88831.089 1.00 50.08 C C

ATOM 5861SD METC 1470.181 -17.7_1231.519 1.00 54.58 C S

ATOM 5862CE METC 1470.120 17.50533.303 1,00 53.86 C C

ATOM 5863C METC 147-1.896 -13.56329.192 1.00 44.11 C C

ATOM 5864O METC 147-1.546 -12.47529.655 1.00 42.40 C O

ATOM 5865N THRC 148-1.943 -13.82227.888 1.00 43.26 C N

ATOM 5866CA THRC 148-1.572 -12.81926.903 1.00 43.33 C C

ATOM 5867CB THRC 148-1.459 -13.44425.505 1.00 43.47 C C

ATOM 5868OG1THRC 148-0.415 -14.42525.524 1.00 44.71 C 0 ATOM 5869CG2THRC 148-1.137 -12.38524.455 1,00 42.65 C C

ATOM 5870C THRC 14B-2.562 -11.66426.884 1.00 42.33 C C

ATOM 5871O THRC 148-2.157 -10.51526.960 1.00 41.90 C O

ATOM 5872N LEUC 149-3.854 -11.96826.793 1,00 42.36 C N

ATOM 5873CA LEUC 149-4.878 -10.92826.788 1.00 41.89 C C

ATOM 5874CB LEUC 149&.268 -11.55026.814 1.00 41.38 C C

ATOM 5875CG LEUC 149-7.429 -10.57627.032 1.00 42.80 C C

ATOM 5576CD1LEUC 149-7.528 -9.60825.848 1.00 42.25 C C

ATOM 5877CD2LEUC 149-8.731 -11.37027.184 1.00 41.18 C C

ATOM 5878C LEUG 149-4.715 -10.01228.002 1.00 42.41 C C

ATOM 5879O LEUC 149-4.628 -8.78727.860 1.00 43.13 C O

ATOM 5880N GLUC 150-4.664 10.61629.188 1.00 41.65 C N

ATOM 5881CA GLUC 150X1.521 -9.87530.441 1.00 41.25 C C

ATOM 5882CB GLUC 150-4.606 -10.85431.627 1.00 42.07 C C

ATOM 5883CG GLUC 150-4.434 -10.24533.022 1.00 41.55 C C

ATOM 5884CD GLUC 150-4.917 -1_1.17934.150 1.00 43.50 C C

ATOM 5885OE1GLUC 150-4.613 -12.394_34.1071.00 43.73 C 0 ATOM 5886OE2GLUC 150-5.593 -10.69435.087 1.00 41.91 C 0 ATOM 5887C GLUC 150-3.213 -9.08030.478 1.00 40.67 C C

ATOM 5888O GLUC 150-3.118 -8.05031.153 1.00 38.96 C O

ATOM 5889N ASPC 151-2.207 -9.56529.756 1.00 40.46 C N

ATOM 5890CA ASPC 151-0.922 -8.88229.696 1.00 41,33 C C

ATOM 5891CB ASPC 1510.148 -9.81429.117 1.00 44.02 C C

ATOM 5892CG ASPC 1510.817 -10.68330.184 1.00 46.74 C C

ATOM 5893OD1ASPC 1511.472 -11.68729.813 1.00 48.15 C O

ATOM 5894OD2ASPC 1510.702 -10.35731.388 1.00 47.14 C O

ATOM 5895C ASPC 151-1.069 -7.62428.829 1.00 41.14 C C

ATOM 5896O ASPC 151-0.269 -6.68528.927 1.00 41.30 C O
' ATOM 5897N HISC 152-2.103 -7.60527.993 1.00 38.85 C N

ATOM 5898CA HISC 152-2.350 -6.45827.145 1.00 38.91 C C

ATOM 5899CB HISC 152-2.797 -6.91025.758 1.00 40.38 C C

ATOM 5900CG HISC 152-1.655 -7.30624.875 1.0D 42.11 C C

ATOM 5901CD2HISC 152-1.243 -6.82323.679 1.00 42.57 C C

ATOM 5902ND1HISC 152-0.743 -8.27825.230 1.00 43.52 C N

ATOM 5903CE1HIS' 1520.184 -8.37424.293 1.00 43.31 C C
C

ATOM 5904NE2HIS! 152-0.096 -7.50223.340 1.00 43.43 C N
C

ATOM 5905C HIS' 152-3.332 -5.46527.757 1.00 38.08 C C
C

ATOM 5906O HISC 152-3.875 -4.600_ 1.00 36.98 C O
27.069 ATOM 5907N TYRC 153-3.572 -5.62329.056 1.00 36.48 C N

ATOM 5908CA TYRC 153x.403 -4.69229.807 1.00 36.16 C C

ATOM 5909CB TYRC 153-5.343 -5.41730.787 1.00 33.40 C C

ATOM 5910CG TYRC 153-6.735 -5.64930.243 1.00 29.90 C C

ATOM 5911CD1TYRC 153-7.051 -6.80729.533 1.00 29.81 C C

ATOM 5912CE1TYRC 153-8.323 -6.98828.969 1.00 26.99 C C

ATOM 5913CD2TYRC 153-7.725 -4.67930:383 1.00 29.33 C C

ATOM 5914CE2TYRC 153-8.998 -4.84929.821 1.0D 26.21 C C

ATOM 5915CZ TYRC 153-9.287 -6.00029.117 1.00 26.34 C C

ATOM 5916OH TYRC 153-10.534-6.14928.536 1.00 24.96 C O

ATOM 5917C TYRC 153-3.322 -3.91030.565 1.00 37.51 C C

ATOM 5918O TYRC 153-2.302 -4.48830.956 1.00 38.27 C O

ATOM 5919N HiSC 154-3.521 -2.61230.776 1.00 38.62 C N

ATOM 5920CA HISC 154-2.494 -1.81731.445 1.00 39.07 C C

ATOM 5921CB HISC 154-2.541 -0.35830.959 1.00 40.02 C C

ATOM 5922CG HISC 154-2.445 -0.19929.470 1.00 42.10 C C

ATOM 5923CD2HISC 154-2.443 -1.11028.469 1.00 42.39 C C

ATOM 5924ND1HISC 154-2.343 1.036 28.862 1.00 42.93 C N

ATOM 5925CE1HISC 154-2.281 0.875 27.552 1.00 43.32 C C

ATOM 5926NE2HISC 154-2.341 -0.41727.288 1.00 43.35 C N

ATOM 5927C HISC 154-2.549 -1.83432.966 1.00 39.29 C C

ATOM 5928O HISC 154-3.521 -1.39533.573 1.00 38.39 C O

ATOM 5929N ALAC 155-1.470 -2.30633.576 1.00 41.04 C N

ATOM 5930CA ALAC 155-1.368 -2.37635.031 1.00 43.05 C C

ATOM 5931CB ALAC 155-0.154 -3.22935.423 1.00 44.28 C C

ATOM 5932C ALAC 155-1.270 -0.99635.692 1.00 43.53 C C

ATOM 5933O ALAC 155-1.527 -0.85536.890 1.00 43.59 C O

ATOM 5934N ASPC 156-0.902 0.017 34.913 1.00 43.11 C N

ATOM 5935CA ASPC 156-0.767 1.379 35.428 1.00 42.65 C C

ATOM 5936CB ASPC 1560.287 2.136 34.622 1.00 42.88 C C

ATOM 5937CG ASPC 156-0.085 2.261 33.158 1.00 43.27 C C

ATOM 5938OD1ASPC 156-0.225 1.216 32.491 1.00 45.26 C O

ATOM 5939OD2ASPC 156-0.247 3.399 32.670 1.00 45.56 C O

ATOM 5940C ASPC 156-2.080 2.151 35.352 1.00 43.07 C C

ATOM 5941O ASPG 156-2.127 3.347 35.654 1.00 44.40 C O

ATOM 5942N VALC 157-3.142 1.474 34.933 1.00 41.32 C N

ATOM 5943CA VALC 157-4.443 2.112 34.808 1.00 40.21 C C

ATOM 5944CB VALC 157-5.075 1.771 33.427 1.00 41.41 C C

ATOM 5945CG1VALC 157-6.449_2.389 33.298 1.00 41.49 C C

ATOM 5946CG2VALC 157-4.166 2.289 32.309 1.00 40.60 C C

ATOM 5947C VALC 157-5.333 1.645 35.956 1.00 39.34 C C

ATOM 5948O VALC 157-5.641 0.461 36.087 1.00 39.35 C O

ATOM 5949N ALAC 158-5.745 2.592 36:788 1.00 38.32 C N

ATOM 5950CA ALAC 158-6.563 2.298 37.959 1.00 37.12 C .
C

ATOM 5951C8 ALAG 158-6.852 3.590 38.711 1.00 36.79 C C

ATOM 5952C ALAC 158-7.865 1.545 37.708 1.00 36.74 C C

ATOM 5953O ALAC 158-5.162 0.574 38.412 1.00 36.43 C O

ATOM 5954N TYRC 159-8.635 1.981 36.714 1.00 35.77 C N

ATOM 5955CA TYRC 159-9.913 1.352 36.415 1.00 35.15 C C

ATOM 5956CB TYRC 159-10.9602.435 36.157 1.00 35.75 C C

ATOM 5957CG TYRC 159-12.3661.914 36.038 1.00 36.34 C C

ATOM 5958CD1TYRC 159-13.1191.619 37.173 1.00 37.75 C C

ATOM 5959CE1TYRC 159-14.4121.101 37.071 1.00 36.70 C C

ATOM 5960CD2TYRC 159-12.9411.683 34.789 1.00 36.35 C C

ATOM 5961CE2TYRC 159-14.2331.164 34.674 1.00 37.01 C C

ATOM 5962CZ TYRC 159-14.9580.875 35.822 1.00 36.95 C C

ATOM 5963OH TYRC 159-16.2140.336 35.717 1.00 36.70 C O

ATOM 5964C TYRC 159-9.897 0.359 35.243 1.00 36.30 C C

ATOM 5965O TYRC 159-10.070-0.84235.454 1.00 36.60 C O

ATOM 5966N HISC 160-9.703 0.847 34.013 1.00 35.83 C N

ATOM 5967CA HISC 160-9.691 -0.03532.838 1.00 35.19 C C

ATOM 5968CB HISC 160-9.775 0.773 31.542 1.00 34.71 C C

ATOM 5969CG HIS C 160-10,9291,723 31.4981.00 34.81 C C

ATOM 5970CD2HIS C 160-12.1991.574 31.0331.00 34.12 C C

ATOM 5971ND1HIS C 160-10.8642.996 32.0211.00 36.12 C N

ATOM 5972CE1HIS C 160-12.0343.591 31.8821.00 33.82 C C

ATOM 5973NE2HIS C 160-12.8572.749 31.2861.00 33.94 C N

ATOM 5974C HIS C 160-8.473 -0.94932.7631.00 34.89 C C
ATOM 5975O HIS C 160-7.584 -0.74231.9361.00 35.42 C O

ATOM 5976N ASN C 161-8.455 -1.96733.6191.00 34.94 C N

ATOM 5977CA ASN C 161-7.359 -2,93933.6771.00 34.40 C C

ATOM 5978CB ASN C 161-6.518 -2.70234.9251.00 32.87 C C
ATOM 5979CG ASN C 161-7.374 -2.57536.1731.00 33.72 C C

ATOM 5980OD1ASN ' 161-8.298 -3.36936.3881.00 31.78 C O
C

ATOM 5981ND2ASN . 161-7.074 -1,57937.0011,00 _ C N
C 31.13 ATOM 5982C ASN ~ 161-7.915 -4.36633.7111.00 34.43 C C
C

ATOM 5983O ASN C 161-9,110 -4,59333.4831.00 33.12 C O

ATOM 5984N ASN C 162-7.050 -5.32734.0091.00 35.15 C N

ATOM 5985CA ASN C 162-7.475 -6.71934.0451.00 37.02 C C

ATOM 5986CB ASN C 162-6.258 -7.64234.2011.00 37.67 C C

ATOM 5987CG ASN C 162-5.408 -7.29235.3961.00 39,42 C C

ATOM 5988OD1ASN C 1625.243 -6,12435.7281,00 42.27 C O

ATOM 5989ND2ASN C 162-4.841 -8.30836.0421.00 42,10 C N

ATOM 5990C ASN C 162-8.527 -7.02335.1131.00 37.50 C C

ATOM 5991O ASN C 162-9.349 -7.91934.9281.00 37.04 C O

ATOM 5992N ILE C 163-8.518 -6.27636.2161.00 37.34 C N

ATOM 5993CA ILE C 163-9.492 -6.51337.2731.00 38.01 C C

ATOM 5994CB ILE C 163-9,174 3.697 38.5371.00 38.01 C C

ATOM 5995CG2iLE C 163-10.046-6.18239.6881,00 38,09 C C

ATOM 5996CG1ILE C 163-7.705 -5.86838.9201.00 37.43 C C

ATOM 5997CD1ILE C 163-7.288 -4.95740.0641.00 37.25 C C

ATOM 5998C ILE C 163-10.890-6.14836.7771.00 39.15 C C

ATOM 5999O ILE C 163-11.850-6,89437.0061.00 39.48 C O

ATOM 6000N HIS C 164-11.001-5,00436.0991.00 39.01 C N

ATOM 6001CA HIS C 164-12.282-4,55835,5331.00 39.08 C C

ATOM 6002CB HIS C 164-12.130-3.16634.9061.00 38.15 C C

ATOM 6003CG HIS C 164-13.236-2.80133.9601.00 38.88 C C

ATOM 6004CD2HIS C 164-13.228-2.57632.6241.00 38.05 C C

ATOM 6005ND1HIS C 164-14.541-2.62734,3681,00 39.07 C N

ATOM 6006CE7HIS C 164-15,288-2,31233.3251.00 38.83 C C

ATOM 6007C HIS C 164-12.7525.554 34_.4651.00 38.74 C C

ATOM 60080 HIS C 164-13,945-5.81734.3211.00 39.17 C O

ATOM 6009NE2HIS C 164-14.516-2.27332.2531.00 39.53 C N

ATOM 6010N ALA C 165-11.801-6.10033.7131.00 37.56 C N

ATOM 6011CA ALA C 165-12,119-7,06332,6721,00 36.79 C C

ATOM 6012CB ALA C 165-10.870-7.39731,8661.00 33.99 C C

ATOM 6013C ALA C 165-12,668-8,32033.3331,00 37,26 C C

ATOM 6014O ALA C 165-13.722-8.83332.9471.00 37.41 C O

ATOM 6015N ALA C 166-11.939-8.80734.3331.00 37.23 C N

ATOM 6016CA ALA C 166-12.335-9.99735.0591.00 37.19 C C

ATOM 6017CB ALA C 166-11.348-10,27336.1851.00 35,90 C C

ATOM 6018C ALA C 166-13.729-9.77635.6201.00 37.99 C C

ATOM 6019O ALA C 166-14.593-10.64435,5211.00 39.14 C O

ATOM 6020N ASP C 167-13.949-8.58936.1781.00 37.88 C N

ATOM 6021CA ASP C 167-15.226-8.24936.7811.00 37.37 C C

ATOM 6022CB ASP C 167-15.114-6.90337.4961.00 38.20 C C

ATOM 6023CG ASP C 167-16,401-6,50538.1771.00 39.40 C C
.

ATOM 6024OD1ASP C 167-17,054-7,39138.7651.00 42.50 C O

ATOM 6025OD2ASP C 167-16.763-5.31138.1391.00 40.54 C O

ATOM 6026C ASP C 167-16.428-8,23735.8381.00 38.23 C C

ATOM 6027O ASP C 167-17.501-8.71436.1971.00 37.80 C 0 ATOM 6028N VAL C 168-16.260-7.68034.6421.00 37.81 C N

ATOM 6029CA VAL C 168-17.350-7.62133.6791,00 35,98 C C

ATOM 6030CB VAL C 168-17.014-6.65532.5111.00 35.54 C C

ATOM 6031CG1VAL C 168-18.074-6.74231.4251.00 32,87 C C

ATOM 6032CG2VAL C 168'-16.9185.224 33.0431.00 33.31 C C

ATOM 6033C VAL C 168-17.618-9.02033.1521.00 36.59 C C

ATOM 6034O VAL G 168-18.762-9.37732.8651.00 35.81 C O

ATOM 6035N VAL C 169-16.556-9,81133.0341.00 37.53 C N

ATOM 6036CA VAL C 169-16.673-11.18932.5761.00 38,49 C C

ATOM 6037CB VAL C 169-15,290-11,86432.4881,00 _ C C
38.79 ATOM 6038CG1VAL C 169-15.406-13.35932.7521.00 37.43 C C

ATOM 6039CG2VAL C 169-14.697-11.63031.9161.00 39.34 C C

ATOM 6040C VAL C 169-17.532-11.97233.5651.00 39.28 C C

ATOM 6041O VAL C 169-18.538-12.58333.1921.00 38.03 C O

ATOM 6042N GLN C 170-17.115-11.93534.8281.00 40.16 C N

ATOM 6043CA GLNC 170-17,800-12.6333 1.00 42.30 C C
5.

ATOM 6044CB GLNC 170-16.991-12.472_ 1.00 43.65 C C
_ _ 37.201 ATOM 6045CG GLNC 170-17.466-13.29238.3891.00 46.50 C C

ATOM 6046CD GLNC 170-18.583-12.61639.1561.00 48.15 C C

ATOM 6047OE1GLN C 170-18,601-11.39439.3011.00 48.93 C O

ATOM 6048NE2GLN C 170-19.515-13.41239.6691.00 50,06 C N

ATOM 6049C GLN C 170-19.239-12.15036.1001.00 42.05 C C

ATOM 6050O GLN C 170-20.121-12.94736.4361.00 41.75 C 0 ATOM 6051N SER C 171-19.476-10.85835.8621.00 41.53 C N

ATOM 6052CA SER C 171-20.813-10.27436.0061.00 42.23 C C

ATOM 6053CB SER C _1_71-20.748-8.74635.9721.00 41,11 C C

ATOM 6054OG SER C 17~-20.137.x.233 37.1411 00 42 C O
~ ~ ~ ~ ~ 41 AT(M 6055 C SER C 171 -21.734 -10757 R6.RR9 1 AA d7 93 C C
ATOM6056O SERC 171-22.897-11.07935,133 1,00 42,87 C O

ATOM6057N THRC 172-21.204-10.79633.685 1.00 44.36 C N
ATOM6058CA THRC 172-21.973-11.26332.546 1.00 45.95 C C

ATOM6059CB THRC 172-21.165-11.10431.231 1.00 45.79 C C
ATOM6060OG1THRC 172-21.021-9.71030.927 1.00 44.15 C O

ATOM6061CG2THRC 172-21.873-11.80530,075 1.00 45,99 C .
C

ATOM6062C THRC 172-22.306-12,73832.789 1,00 46,54 C C

ATOM6063O THRC 172-23.410-13.19032.505 1.00 47.27 C O
ATOM6064N HISC 173-21.339-13.47033.332 1.00 47.43 C N

ATOM6065CA HISC 173-21.500-14.88833.641 1.00 48.02 C C

ATOM6066CB HISC 173-20.238-15.39934.337 1.00 48.23 C C

ATOM6067CG HISC 173-20.395-16.74934.959 1,00 49,38 C C

ATOM6068CD2HISC 173-20.332-17,14636,252 1,00 48.89 C C

ATOM6069N01HISC 173-20.667-17.88234.222 1.00 49.97 C N

ATOM6070CE1HISC 173-20.765-18.91935.036 1.00 49.94 C C
ATOM6071NE2HISC 173-20.566-18.49936.273 1.00 49.55 C N

ATOM6072C HISC 173-22.724-15.12934.534 1.00 48.48 C C

ATOM6073O HISC 173-23.498-16.06334.311 1.00 47.73 C O

ATOM6074N VALC 174-22.892-14.27635,540 1.00 48.87 C N

ATOM6075CA VAL' 174-24.016-14.39636.462 1.00 49.55 C C
C

ATOM6076GB VAL' 174-23.789-13.54637.741 1.00 49.01 C C
ATOM6077CG1VALC 174-24.997-13.64738.648 1.00 49.12 C C
.
C

ATOM6078CG2VAL' 174-22.539-14.02238.474 1.00 47.62 C C
C

ATOM6079C VALC 174-25.317-13.95735:789 1.00 49.83 C C

ATOM6080O VALC 174-26.363-14,58835.974 1.00 49,87 C O

ATOM6081N LEUC 175-25.246-12.88135.009 1.00 50.06 C N

ATOM6082CA LEUC 175-26.414-12.36434.297 1.00 50.29 C C

ATOM6083CB LEUC 175-26.038-11.09833.526 1.00 50 .51C C

ATOM6084CG LEUC 175-25.708-9.87934:388 1.00 51 .20C C
ATOM6085CD1LEUC 175-24.890-8.87633.591 1.00 51 ,02C C

ATOM6086CD2LEUC 175-26.999-9.25834.900 1,00 51.40 C C

ATOM6087C LEUC 175-26.952-13.42133.332 1.00 50.48 C C

ATOM6088O LEUC 175-28.166-13.52233.117 1.00 49.87 C O
ATOM6089N LEUC 176-26.034-14.20132.761 1.00 50.09 C N
ATOM6090CA LEUC 176-26.379-15.26531.827 1.00 51.55 C C

ATOM6091CB LEUC 176-25.111-15.86131.204 1,00 50.52 C C

ATOM6092CG LEUC 176-24.394-15.13630.060 1.00 49.18 C C

ATOM6093CDtLEUC 176-23,206-16.96929.605 1.00 47.88 C C
ATOM6094CD2LEUC 176-25.346-14.92428.896 1.00 49.31 C C

ATOM6095C LEUC 176-27.176-16.39032.493 1.00 52.50 C C
ATOM6096O LEUC 176-28.031-17.00731.865 1.00 53.15 C O

ATOM6097N SERC 177-26.892-16.65033.763 1.00 53,71 C N

ATOM6098CA SERC 177-27,569-17.70934.499 1.00 54,94 C C

ATOM6099CB SERC 177-26.665-18.24435.612 1.00 54.69 C C

ATOM6100OG SERC 177-25.556-18.94535.082 1.00 54.84 C O

ATOM6101C SERC 177-28.885-17.26335.106 1.00 56.38 C C
ATOM6102O SERC 177-29.477-17.98435.907 9.00 56.96 C O

ATOM6103N THRC 178-29.347-16.07634.740 1.00 57,72 C N

ATOM610_4CA THRC 178-30.604-15.60035.286 1.00 58,79 C C

ATOM6105CB THRC 178-30.898-14.15034,841 1.00 58,56 C C

ATOM6106OG1THRC 178-31.688-13.5D135.842 1.00 57.60 C O

ATOM6107CG2THRC 178-31.651-14.12133.520 1.00 59.13 C C

ATOM6108C THRC 178-31.696-16.55034.796 1.00 59.74 C C

ATOM6109O THRC 178-31.673-16.99033.643 1,00 59.48 C O

ATOM6110N PROC 179-32.650-16.90035.681 1.00 61.11 C N

ATOM6111CD PROC 179X2,630 -16.50237.102 1.00 61,79 C C

ATOM6112CA PROC 179-33.783-17.80235.413 1.00 61.61 C C

ATOM6113CB PROC 179-34.577-17.75336.718 1.00 61.72 C C

ATOM6114CG PROC 179-33.502-17.56237.751.1.00 61.85 C C

ATOM6115C PROC 179-34.649-17.43934.203 1.00 62,01 C C

ATOM6116O PROC 179-35.034-18,31133.421 1.00 62,42 C O

ATOM6117N ALAC 180-34.953-16.15534,051 1,00 62.38 C N

ATOM6118CA ALAC 180-35.777-15.69832.939 1.00 63.26 C C

ATOM6119CB ALAC 180-36.157-14.23533.141 1.00 63.36 C C

ATOM6120C ALAC 180-35.104-15.87731.578 1.00 64.12 C C

ATOM6121O ALAC 180-35,746-15.69830.538 1,00 64.30 C O

ATOM6122N LEUC 18133.818 -16.22531.581 1.00 64.31 C N

ATOM6123CA LEUC 181-33.075-16.41730.333 1,00 64.71 C C

ATOM6124CB LEUC 181-31.885-15.45430.268 1.00 64.79 C C

ATOM6125CG LEUC 181-32.189-13.96230.159 1.00 64.43 C C

ATOM6126CD1LEUC 181-30.902-13.17430.291 1.00 65.11 C C

ATOM6127CD2LEUC 181-32,861-13.67028.829 1.00 64,61 C C

ATOM6128C LEUC 181-32.571-17.84630.195 1.00 64.69 C C

ATOM6129O LEUC 181-31.894-18.19229.228 1,00 65.00 C O

ATOM6130N G_LUC 182-32.905-18.67531.171 1.00 65.01 C N

ATOM6131CA GLUC 182-32.481-20.06531.167 1.00 64.88 C C

ATOM6132CB GLUC 182-33.104-20.77332.372 1.00 66.95 C C

ATOM6133CG GLUC 18232.718 -22.23032.548 1.00 69.56 C C

ATOM6134CD GLUC 182-33,044-22.73533.945 1.00 71,32 C C

ATOM6135OE1GLUC 182-34.188-22,51434.409 1.00 71.74 C O

ATOM6136OE2GLUC 182-32.157-23.35134.577 1.00 73.16 C O

ATOM6137C GLUC 182-32.843-20.78429.864 1.00 63.84 C C

ATOM6138O GLUC 182-33.973-20.69329.380 1.00 63.44 C O

ATOM6139N ALAC 183-31,860-21.48029.297 1.00 62.56 C N

ATOM6140CA ALAC 183-32.029-22.24428 059 1 61 C C
I I I I I ( ~ ~ ~ 00 31 ATOM 6141CB 183-33.219-23.198-28.2031.00 61.62 C C
ALA
C

ATOM 6142C 183-32.186-21.41126.7821.D0 59.85 C C
ALA
C

ATOM 61430 183-32.220-21.96125.6781.00 58.91 C O
ALA
C

ATOM 6144N 184-32.269-20.09226.9321 58 C N

C

ATOM 6145CA VAL 184-32.444-19.19425.790. . C C
C 1.00 57.26 ATOM 6146CB VAL 184-32.525-17.77426.2571.00 57.38 C C
C

ATOM 6147CG1VAL 184-33.131-16.89525.0531.00 57.99 C C
C

ATOM 6148CG2VAL 184-34.015-17.83827.1851.00 56.84 C C
C

ATOM 6149C VAL 184-31.252-19.06124.8371 55 C C

ATOM 6150O VALC 18431.440 -18.93623.631. . C O
1.00 55.05 ATOM 6151N PHEC 185-30.032-19.08125.3651.00 55.00 C N

ATOM 6152CA PHEC 185-28.850-18.92824.5141.00 54.29 C C

ATOM 6153CB PHEC 185-27.919-17.85725.1001.00 51.94 C C

ATOM 6154CG PHEC 185-28.540-1fi.49125.1651.00 50.50 C C

ATOM 6155CD1PHEC 185-28.909-15.82423.9991.00 50 C C

ATOM 6156CD2PHEC 185-28.784-15.88026.3891.00 . C C
50.19 ATOM 6157CEtPHEC 185-29.518-14.56324.0511.00 49.76 C C

ATOM 6158CE2PHEC 185-29.393-14.62126.4541.00 50.05 C C

ATOM 6159CZ PHEC 185-29.762-13.96125.2761.00 49.38 C C

ATOM 6160C PHEC 18528.065 -20.21324.2711.00 54.57 C C

ATOM 6161O PHEC 185-28.019-21.10425.1261.00 54 C O

ATOM 6162N THRC 186-27.449-20.29423.0921 . C N

ATOM 6163CA THRC 186-26.649-21.45222.698. . C C
1.00 54.21 ATOM 6164CB THRC 186-26.443-21.48921:1891.00 54.13 C C

ATOM 6165OG1THRC 186-25.525-20.45020.8211.00 54 C O

ATOM 6166CG2THRC 186-27.767-21.27720.4601.00 . C C
53.01 ATOM 6167C THRC 186-25.268-21.36423.3321.00 55.15 C C

ATOM 6168O THRC 186-24.916-20.34323.9261 54 C O

ATOM 6169N ASPC 187-24.479-22.42823.199. . C N
1.00 55.57 ATOM 6170CA ASPC 187-23.131-22.43223.7591.00 55.56 C C

ATOM 6171CB ASPC 187-22.473-23.81823.6381.00 56.59 C C

ATOM 6172CG ASPC 187-23.112-24.85924.5441.00 57.64 C C

ATOM 6173OD1ASPC 187-23.441-24.53625.7061 56 C O

ATOM 6174OD2ASPC 187-23.268-26.01324.091. . C O
1.00 59.12 ATOM 6175C ASPC 187-22.263-21.40523.0351.00 55.16 C C

ATOM 6176O ASPC 187-21.359-20.81323.6281.00 54.06 C O

ATOM 6177N LEUC 188-22.544-21.19921.7511.00 54.15 C N

ATOM 6178CA LEUC 188-21.778-20.25020.9591.00 53.72 C C

ATOM 6179CB LEUC 188-22.072-20.44519.4681 53 C C

ATOM 6180CG LEUC 188-21.118-19.74318.496. . C C
1.00 52.61 ATOM 6181CD1LEUC 188-19.751-20.40818.5551.00 51.51 C C

ATOM 6182CD2LEUC 188-21.682-19.81117.0911.00 51 C C

ATOM 6183C LEUC 188-22.072-18.80321.3731.00 . C C

ATOM 6184O LEUC 188-21.149-18.00921.5521.00 . C O
52.48 ATOM 6185N GLUC 189-23.351-18.46821.5301.00 23 C N

ATOM 6186CA GLUC 189-23.746-17.11821.9291.00 . C C
51.86 ATOM 6187CB GLUC 189-25.261-16.96921.8731.00 52.68 C C

ATOM 6188CG GLUC 189-25.882-17.41320.5731.00 55.16 C C

ATOM 6189CD GLUC 189-27.396-17.45920.6561.00 56.87 C C

ATOM 6190OE1GLUC 189-27.912-18.04821.6311.00 57 C O

ATOM 6191OE2GLUC 189-28.068-16.91619,7491.00 . C O

ATOM 6192C GLUC 189-23.267-16.78623.3441.00 . C C

ATOM 6193O GLUC 189-22.974-15.63123.6561.00 . C O
50.64 ATOM 6194N ILEC 190-23.207-17.79724.2041.00 49.59 C N

ATOM 6195CA ILEC 190-22.748-17.60925.5711.00 48.33 C C

ATOM 6196CB ILEC 190-23.142-18.80526.4731.00 47.79 C C

ATOM 6197CG2ILEC 190-22.242-18.87427.7001.00 47.07 C C

ATOM 6198CGtILEC 190-24.615-18.67826.8881.00 48 C C

ATOM 6199CD1ILEC 190-25.121-19.81127.7821.00 . C C
46.01 ATOM 6200C ILEC 190-21.230-17.41525.5681.00 47 C C

ATOM 6201O ILEC 190-20.694-16.61126.3291.00 . C O

ATOM 6202N LEUC 191-20.545-18.16424.7101.00 . C N
47.39 ATOM 6203CA LEUC 191-19.096-18.06324.5971.00 47.50 C C

ATOM 6204CB LEUC 191-18.548-19.15123.6771.00 46.98 C C

ATOM 6205CG LEUC 191-17.063-19.03023.3091.00 48 C C

ATOM 6206CD1LEUC 191-16.209-19.29424.5451.00 . C C

ATOM 6207CD2LEUC 191-16.712-20.02122 1 . C

. . . C
ATOM 6208C LEUC 191-18.744-16.69524.0151.00 48 C C

ATOM 6209O LEUC 191-17.636-16.19524.2141.00 . C O

ATOM 6210N ALAC 192-19.695-16.09623 1 . C

. . . N
ATOM 6211CA ALAC 192-19.488-14.79422 1 46 C

. . . C
ATOM 6212CB ALAC t92-20.528-14.56121 1 46 C

. . . C
ATOM 6213C ALAC 192-19.552-13 23 1 . . . 46.54 C C
ATOM 6214O ALAC 192-18.638-12 23 . . 1.00 46.74 C O

. . 24.4881.00 45.62 C N

. -12.59225.4951.00 44.30 C C

193-22.165-12.75726.1561.00 45.16 C C

ATOM fi218C ALAC 193-19.715-12.63226.5441.00 44 C C

ATOM 62190 ALAC 193-19.388-11.61527.1721 . C O

ATOM 6220N ILEC 194-19.134-13.81226 . . C

. . . N
ATOM 6221CA ILEC 194-18.080-13 27 1 . . . 43.35 C C
ATOM 6222CB ILEC 194-18.054-15 28 . . 1.00 44.00 C C
ATOM 6223CG2ILEC 194-16.778-15 28 . . 1.00 43.09 C C
ATOM 6224CGtILEC 194-19 -15 , . 29.0011.00 44.66 C C

. -17.08729.6921.00 45.62 C C
ATOM

6226C ILEC 194-16.729-13 27 1 . , , 42.68 C C

ATOM 6227O ILEC 194-15.988-12.8342 1.00 42.21 C O
7.833 ATOM 6228N PHEC 195-16.423-13.950_ 1.00 42.32 C N
_ 25.927 ATOM 6229CA PHEC 195-15.168-13.569_ 25.2821.00 40.87 C C

ATOM ' CB PHEC 195-15.025-14.25323.9191.00 40.85 C C

ATOM 6231CG PHEC 195-13.701-14.00323.2431.00 39.13 C C

ATOM 6232CD1PHEC 195-12.519-14.513_ 1.00 39.14 C C
23.782 ATOM 6233CD2PHEC 195-13.635-13.24622.0741.00 38.94 C .
C

ATOM 6234CE1PHEC 195-11.284-14.27323.1701.00 38.61 C C

ATOM 6235CE2PHEC 195-12.410-12.99621.4501.00 38.47 C C

ATOM 6236CZ PHEC 195-11.230-13.51021.9991.00 38.60 C C

ATOM 6237C PHEC 195-15.193-12.06625.0821.00 40.70 C C

ATOM 6238O PHEC 195-14.220-11.38225.3681.00 41.96 C O

ATOM 6239N ALAC 196-16.319-11.55924.5901.00 39.74 C N

ATOM 6240CA ALAC 196-16.479-10.13124.3591.00 39.13 C C

ATOM 6241CB ALAC 196-17.900-9.83023.9231.00 38.30 C C

ATOM 6242C ALAC 196-16.147-9.34325.6301.00 39.48 C C

ATOM 6243O ALAC 196-15.380-8.37825.5901.00 37.75 C O

ATOM 6244N SERC 197-16.733-9.7682 1.00 38.84 C N
6.750 ATOM 6245CA SERC 197-16.522-9.118_ 1.00 38.34 C C
_ 28.038 ATOM 6246CB SERC 197-17.354-9.80729.1351.00 40.11 C C

ATOM 6247OG SERC 197-18.752-9.66728.9121.00 42.74 C O

ATOM 6248C SERI 197-15.060-9.14828.4321.00 36.78 C C
C

ATOM 6249O SER' 197-14.549-8,19229.0031.00 37.41 C O
C

ATOM 6250N ALAC 198-14.390-10.24928.1201.00 35.49 C N

ATOM 6251CA ALAC 198-12.985-10.40728.4641.00 35.30 C C

ATOM 6252CB ALAC 198-12.549-11.84328.2011.00 34.94 C C

ATOM 6253C ALAC 198-12.063-9.44227.7171.00 35.69 C C

ATOM 6254O ALAC 198-11.040-9.02128.2531.00 36.06 C O

ATOM 6255N ILEC 199-12.438-9.08126.4941,00 34.86 C N

ATOM 6256CA ILEC 199-11.629-8.19625.6641.00 34.87 C C

ATOM 6257CB ILEC 199-11.448-8.80024.2441.00 35.65 C C

ATOM 6258CG2ILEC 199-10.973-10.246_ 1:00 36.12 C C
24.339 ATOM 6259CG1ILEC 199-12.779-8.748_ 1.00 34.42 C C
23.478 ATOM 6260CD1ILEC 199-12.643-9.03821.9961.00 35.18 C C

ATOM 6261C ILEC 199-12.232-6.80025.4771.00 35.16 C C

ATOM 6262O ILEC 199-11.626-5.94424.8351.00 35.70 C O

ATOM 6263N HISC 200-13.403-6.55726.0521.00 34.70 C N

ATOM 6264CA HISC 200-14.074-5.27925.8361,00 35.01 C C

ATOM 6265CB HISC 200-15.427-5.24626.5731.00 33.97 C C

ATOM 6266CG HISC 200-15.373-4.59327.9171.00 34.14 C C

ATOM 6267CD2HISC 200-15.670-3.33028.3051.00 33.37 C C

ATOM 6268ND1HISC 200-14.942-5.25129.0491.00 33.55 C N

ATOM 6269CE1HISC 200-14.974-4.41930.0761.00 34.04 C C

ATOM 6270C HISC 200-13.289-3.99226.1171.00 34.02 C C

ATOM 6271O HISC 200-13.673-2.93025.6391.D0 33.94 C O

ATOM 6272NE2HISC 200-15.411-3.24629.6511.00 35.61 C N

ATOM 6273N ASPC 201-12.204-4.06826.8721.00 32.99 C N

ATOM 6274CA ASPC 201-11.420-2.86727.1561.00 33.16 C C

ATOM 6275CB ASPC 201-11.727-2.31828.5531.00 36.63 C C

ATOM 6276CG ASPC 201-12.996-1.49428.6051.00 39.97 C C

ATOM 6277C ASPC 201-9.927 -3.13627.0911.00 30.79 C C

ATOM 6278O ASPC 201. -9.146-2.42327.7121.00 29.51 C O

ATOM 6279OD1ASPC 201-13.365-0.87127.5841.00 46.75 C O

ATOM 6280OD2ASPC 201-13.617-1.45529.6901.00 42.72 C O

ATOM 6281N VALC 202-9.519 -4.15326.3461.00 29.01 C N

ATOM 6282CA VALC 202-8.103 -4.47126.3081.00 29.33 C C

ATOM 6283CB VALC 202-7.855 -5.82125.5951.00 28.26 C C

ATOM 6284CG1VALC 202-8.118 -5.69224,1211.00 29.19 C C

ATOM 6285CG2VALC 202-6.447 -6.30925.8741.00 29.73 C C

ATOM 6286C VALC 202-7:261 -3.35225.6861.00 29.35 C C

ATOM 6287O VALC 202-7.685 -2.66124.7451.00 28.07 C O

ATOM 6288N ASPC 203-6.079 -3.17326.2651.00 29.61 C N

ATOM 6289CA ASPC 203-5.117 -2.16625.8531.00 30.40 C C

ATOM 6290CB ASPC 203-4.641 -2.44524.4211.00 31.24 C C

ATOM 6291CG ASPC 203-3.357 -1.71224.0791.00 32.93 C C

ATOM 6292OD1ASPC 203-2.440 -1.69124.9281.00 31.91 C O

ATOM 6293OD2ASPC 203-3.260 -1.16622.9571.00 32.96 C O

ATOM 6294C ASPC 203-5.693 -0.76125.9771.00 30.61 C C

ATOM 6295O ASPC 2035.325 0.140 25.2301.00 31.15 C O

ATOM 6296N HISC 204-6.601 -0.57426.9351.00 30.05 C N

ATOM 6297CA HISC 204-7.201 0.739 27.1631.00 28.37 C C

ATOM 6298CB HISC 204-5.323 0.619 28.1811.00 26.57 C C

ATOM 6299CG HISC 204-9.184 1.837 28.2911.00 26.91 C C

ATOM 6300CD2HISC 204-10.5032.021 28.0361.00 25.70 C C

ATOM 6301ND1HISC 204-8.711 3.045 28.7511.00 26.76 C N

ATOM 6302CE1HISC 204-9.700 3.922 28.7761.00 26.85 C C

ATOM 6303NE2HISC 204-10.7983.326 28.3461.00 25.92 C N

ATOM 6304C HISC 204-6.096 1.668 27.6791.00 29.88 C C

ATOM 6305O NISC 204-5.383 1.344 28.6341.00 28.72 C O

ATOM 6306N PROC 205-5.938 2.841 27.0471.00 30.51 C N

ATOM 6307CD PROC 205-6.708 3.351 25.8951.00 28.86 C C

ATOM 6308CA PROC 205-4.902 3.797 27.4581.00 29,46 C C

ATOM 6309CB PROC 205-4.799 4.729 26.2521.00 27.85 C C

ATOM 6310CG PROC 205-6.220 4.796 25.7821,00 28.55 C C

ATOM 6311C PROC 205-5.188 4.554 28.7471.00 29.98 C C

ATOM 63120 PROC 205-4.281 5.122 29.3401.00 30.98 C O

ATOM 6313N GLYC 206-6.4384.572 _ 29.1881.00 29.71 C N

ATOM 6314CA GLYC 206-6.7465.291 __ 1.00 29.78 C C
30.413 ATOM 6315C GLYC 206-7.2856.688 __ 1.00 30.44 C C
30.144 ATOM 63160 GLYC 206-7.4107.509 31.0541.00 29.60 C O

ATOM 6317N VALt 207-7.5956.958 28.8781.00 29.97 C N
C

ATOM 6318CA VAL' 207-8.1468.246 28.4661.0D 29.58 C C
C

ATOM 6319CB VAL~ 207-7.0839.135 27.7351.00 28.79 C C
C

ATOM 6320CG1VALC 207-6.0159.582 28.7121.00 27.52 C C

ATOM 6321CG2VALC 207-6.4518.373 26.5981.00 25.74 C C

ATOM 6322C VALC 207-9.3397.985 27:5351.00 29.96 C C

ATOM 6323O VAL~ 207-9.4126.957 26:8731.00 28.50 C O
C

ATOM 6324N SERC 208-10.2618.935 27.4911.00 31.51 C N

ATOM 6325CA SERC 208-11.4688.820 26.6921.00 32.12 C C

ATOM 6326CB SERC 208-12.4639.877 27.1431.00 33.04 C C

ATOM 6327OG SERC 208-11.96411.163 26.8271.00 36.69 C O

ATOM 6328C SERC 208-11.2658.955 25.1931.00 31.78 C C

ATOM 6329O SER. 208-10.2509.466 24.7381.00 32.39 C O
C

ATOM 6330N ASNC 209-12.2578.494 24.4341.00 31.98 C N

ATOM 6331CA ASNC 209-12.2238.581 22.9841.00 33.10 C C

ATOM 6332CB ASNC 209-13.5698.153 22.3751.00 32.14 C C

ATOM 6333CG ASNC 209-13.7156.650 22.2601.00 31.98 C C

ATOM 6334OD1ASNC 209-12.7695.938 21.9231.00 32.00 C O

ATOM 6335ND2ASNC 209. -14.9186.161 _ 1.00 32.80 C N
22.515 ATOM 6336C ASNC 209-11.92210.024 _ 1.00 33.09 C C
22.562 ATOM 6337O ASNC 209-11.07310.273 21.7091.00 32.85 C O

ATOM 6338N GLNC 210-12,63910.956 23.1751.00 32.52 C N

ATOM 6339CA GLNC 210-12.50912.375 22.8951.00 33.09 C C

ATOM 6340CB GLNC 210-13.48113.164 23.7831.00 32.64 C C

ATOM 6341CG GLNC 210-13.67614.605 23.3531.00 35.89 C C

ATOM 6342CD GLNC 210-14.17714.705 21.9281.00 38.74 C C

ATOM 6343OE1GLNC 210-15.20914.125 21.5791.00 40.08 C O

ATOM 6344NE2GLNC 210-13.44615.436 21.0891.00 40.33 C N

ATOM 6345C GLNC 210-11.09112.925 23.0711.00 32.44 C C

ATOM 6346O GLNC 210-10.68313.842 22.3471.00 31.82 C O

ATOM 6347N PHEC 211-10.35112.385 24.0381.00 31.71 C N

ATOM 6348CA PHEC 211-8.98312.838 24.2871.00 30.38 C C

ATOM 6349CB PHEG 211-8.49612.307 25.6481.00 30.44 C C

ATOM 6350CG PHEC 211-7.06112,644 25.9791.00 27.97 C C

ATOM 6351CD1PHEC 211-6.01811.871 25.4881.00 28.41 C C

ATOM 6352CDZPHEC 211-6.76113.708 26.8191.00 27.90 C C

ATOM 6353CE1PHEC 211-4.68312.156 25.8381.00 29.56 C C

ATOM 6354CE2PHEC 211-5.44614.002 27.1701.00 29.18 C C

ATOM 6355CZ PHEC 211-4.40013.219 26.6761.00 29.28.C C

ATOM 6356C PHEC 211-8.11612.326 23.1371.00 29.54 C C

ATOM 63570 PHEC 211-7.24013.030 22.6501.00 29.93 C O

ATOM 6358N LEUC 212-8.38611.108 22.6921.00 28.48 C N

ATOM 6359CA LEUC 212-7.64510.518 21.5841.00 29.07 C C

ATOM 6360CB LEUC 212-8.0599.055 21.3931.00 27.68 C C

ATOM 6361CG LEUC 212-7.6908.164 22.5851.00 28.38 C C

ATOM 6362CD1LEUC 212-8.2106.757 22.3721.00 25.48 C C

ATOM 6363CD2LEUC 212-6.1688.150 22.7601.00 26.63 C C

ATOM 6364C LEUC 212-7.91011.305 20.2951.00 29.95 C C

ATOM 6365O LEUC 212-6.99811.520 19.4791.00 29.17 C O

ATOM 6366N ILEC 213-9.16511.726 20.1291.00 28.71 C N

ATOM 6367CA ILEC 213-9.59912.499 18.9701.00 28.07 C C

ATOM 6368CB ILEC 213-11.14312.665 18.9701.00 28.49 C C

ATOM 6369CG2ILEC 213-11.57113.714 17.9621.00 26.40 C C

ATOM 6370CG1ILEC 213-11.81211.315 18.6961.00 29.10 C C

ATOM 6371CD1ILEC 213-13.31211.318 18.9301.00 26.91 C C

ATOM 6372C ILEC 213-8.95113.887 18.9841.00 28.51 C C

ATOM 6373O ILEC 213-8.34214.290 18.0071.00 28.64 C O

ATOM 6374N ASNC 214-9.08214.601 20.1001.00 29.47 C N

ATOM 6375CA ASNC 214-8.53715.950 20.2441.00 30.50 C C

ATOM 6376CB ASNC 214-8.87616.532 21.6241.00 30.42 C C

ATOM 6377CG ASNC 214-10.33116.922 21.7621.00 32.37 C C

ATOM 6378OD1ASNC 214-11.11516.839 20.8091.00 33.16 C O

ATOM 6379ND2ASNC 214-10.70417.361 22.9561.00 31.60 C N

ATOM 6380C ASNC 214-7.03316.085 20.0441.00 30.77 C C

ATOM 6381O ASNC 214-6.57517.107 19.5551.00 32.84 C O

ATOM 6382N THRC 215-6.26115.079 20.4421.00 29.81 C N

ATOM 6383CA THRC 215-4.80615.143 20.2991.00 28.72 C C

ATOM 6384CB THRC 215-4.08414.334 21.4521.00 28.25 C C

ATOM 6385OG1THRC 215-4.55912.985 21.4821.00 27.63 C O

ATOM 6386CG2THRC 215-4,35414.948 22.8041.00 26.31 C C

ATOM 6387C THRC 215-4.34414.614 18.9341.00 29.13 C C

ATOM 6388O THRC 215-3.15014.597 18.6311.00 28.74 C O

ATOM 6389N ASNC 216-5.30614.195 18.1151.00 29.71 C N

ATOM 6390CA ASNC 216-5.05213.643 16.7841.00 29.89 C C

ATOM 6391CB ASNC 216-4.25214.618 15,9151.00 31.63 C C

ATOM 6392CG ASNC 216-5.06215.809 15.4851.00 33.56 C C

ATOM 6393OD1ASNC 216-6.29615.727 15.3541.00 35.43 C O

ATOM 6394ND2ASNC 216-4.38316.921 15.2341.00 29.00 C N

ATOM 6395C ASNC 216-4.30912.321 16.8201.00 29.11 C C

ATOM 63960 ASNC 216-3.55712.004 15.8901.00 30.72 C O
ATOM 6397N SERC 217-4.52911.531 17.8621.00 27.03 C N

ATOM 6398CA SERC 217-3.83210.259 17.9701.00 26.83 C C

ATOM 6399CB SERC 217 x.323 9.467 19.189 1.00 27.05 C C

ATOM 6400OG SERC 217 -5.682 9.103 19.075 1.00 26.31 C O

ATOM 6401C SERC 217 -4.016 9.437 16.709 1.00 27.68 C C

ATOM 6402O SERC 217 5.009 9.569 16.001 1.00 28.01 C O

ATOM 6403N GLUC 218 -3.032 8.603 16.424 1.00 29.01 C N

ATOM 6404CA GLUC 218 -3.061 7.737 15.268 1.00 31.58 C C

ATOM 6405CB GLUC 218 -1.769 6.911 15.236 1.00 33.97 C C

ATOM 6406CG GLUC 218 -1.862 5.581 14.485 1.0D 36.34 C C

ATOM 6407CD GLUC 218 -0.548 4.808 14.489 1.00 37.88 C C

ATOM 6408OE1GLUC 218 0.119 4.768 15.544 1.00 40.11 C O

ATOM 6409OE2GLUC 218 -0.189 4.224 13.447 1.0D 38.92 C O

ATOM 6410C GLUC 218 x.285 6.824 15.340 1.00 32.97 C C

ATOM 6411O GLUC 218 -4.874 6.468 14.321 1.00 35.12 C O

ATOM 6412N LEUC 219 -4.664 6.442 16.550 1.00 32.85 C N

ATOM 6413CA LEUC 219 -5.809 5.569 16.747 1.00 32.39 C C

ATOM 6414CB LEUC 219 -5.943 5.266 18.244 1.00 33.14 C C

ATOM 6415CG LEUC 219 -6,201 3.842 18.735 1.00 34,94 C C

ATOM 6416CD1LEUC 219 -5.377 2.820 17.958 1.00 34.36 C C

ATOM 6417CD2LEUC 219-5.850 3.791 20.214 1.00 33.79 C C

ATOM 6418C LEUC 219-7.072 6.255 16.222 1.00 32,10 C C

ATOM 6419O LEUC 219-7.864 5.660 15.486 1.00 32.21 C O

ATOM 6420N ALAC 220 -7.249 7.510 16.608 1.00 30.27 C N

ATOM 6421CA ALAC 220 -8.406 8.278 16.187 1.00 31.15 C C

ATOM 6422CB ALAC 220 -8.426 9.635 16.909 1.00 28.25 C C

ATOM 6423C ALAC 220 -8.424 8.472 14.669 1.00 32.80 C C

ATOM 6424O ALAC 220 -9.488 8.408 14.041 1.0D 33.70 C O

ATOM 6425N LEUC 229 -7.252 8.699 14.075 1.0D 34.32 C N

ATOM 6426CA LEUC 221 -7.170 8.885 12.630 1.00 35.98 C C

ATOM 6427CB LEUC 221 -5.756 9.337 12.216 1.00 36.75 C C

ATOM 6428CG LEUC 221 -5.228 10.63012.885 1.00 40.42 C C

ATOM 6429CD1LEUC 221 -0.005 11.13912.130 1.00 40.64 C C
, ATOM 6430CD2LEUC 221 -6.298 11.71612.905 1.00 40.33 C C

ATOM 6431C LEUC 221 -7.540 7.582 11:930 1.00 36.83 C C

ATOM 6432O LEUC 221 -8.257 7.582 10.936 1.00 37.53 C O
.

ATOM 6433N METC 222 -7,072 6.470 12.481 1.00 37.32 C N
' ATOM 6434CA METC 222 -7.335 5.155 11.918 1,00 39.43 C C

ATOM 6435CB METC 222 -6.554 4.105 12.710 1.00 42.68 C C

ATOM 6436CG METC 222 -6.679 2.683 12.212 1.00 45.84 C C

ATOM 6437SD METC 222 -6.047 2.460 10.536 1.00 54.00 C S

ATOM 6438CE METC 222 -4.232 ' 2.52610.812 1.00 52.63 C C

ATOM 6439C METC 222 -8.820 4.776 __11.88_81,00 38.99 C C

ATOM 6440O METC 222 -9.302 4.215 10.903 1.00 40.51 C O

ATOM 6441N TYRC 223 -9.541 5.091 12.960 1.00 36.76 C N

ATOM 6442CA TYRC 223 -10.9564.747 13.053 1.00 34,13 C C

ATOM 6443CB TYRC 223 -11.2304.108 14.410 1.0D 30.82 C C

ATOM 6444CG Tl'RC 223 -10.5862.754 14.548 1.00 28.05 C C

ATOM 6445CDtTYRC 223 -10.9451.708 13.709 1.00 26,94 C C

ATOM 6446CE1TYRC 223 -10.3480.450 13.521 1.00 27.81 C C

ATOM 6447CD2TYRC 223 -9.612 2.518 15._5121,00 28.06 C C

ATOM 6448CE2TYRC 223 -9.007 1.265 15.639 1.00 28.64 C C

ATOM 6449CZ TYRC 223 -9.379 0.235 14.787 1.00 29.42 C C

ATOM 6450OH TYRC 223 -8.766 -1.00114.885 1.00 30.43 C O

ATOM 6451C TYRC 223 -11.9085.904 12.816 1.00 33.75 C C

ATOM 6452O TYRC 223 -13.0805.850 13.164 1.00 33.23 C O

ATOM 6453N ASNC 224 -11.3876.968 12.232 1.00 _3_4,71C N

ATOM 6454CA ASNC 224 -12.2018.130 11.912 1.00 34.37 C C

ATOM 6455CB ASNC 224 -13.0737.810 10.693 1.00 31.94 C C

ATOM 6456CG ASNC 224 -12.2497.453 9.486 1.00 27.88 C C

ATOM 6457OD1ASNC 224 -11.4218.236 9.051 1.00 28.34 C O

ATOM 6458ND2ASNC 224 -12.4626.269 8.943 1.00 28,82 C N

ATOM 6459C ASNC 224 -13.0658.682 13.028 1.0D 35.03 C C

ATOM 6460O ASNC 224 -14.2498.971 12.811 1.0D 36.96 C O

ATOM 6461N ASPC 225 -12.4708.820 14213 1.00 33.88 C N

ATOM 6462CA ASPC 225 -13.1379.396 15.380 1.00 32.74 C C

ATOM 6463CB ASPC 225 -13.44910.86315.091 1.00 33.15 C C

ATOM 6464CG ASPC 225 -12.19511.68514.817 1.00 36.68 C C

ATOM 6465ODtASPC 225 -11.08711.08814.798 1.00 37.91 C 0 ATOM 6466OD2ASPC 225 -12,31312.92314.626 1.00 35.73 C O

ATOM 6467C ASPC 225 -14.4008.695 15.861 1.00 31.54 C C

ATOM 64680 ASPC 225 -15.1159.203 16.720 1.00 30.12 C O

ATOM 6469N SERC 226 -14.6597.516 15.322 1.00 32,52 C N

ATOM 6470CA SERC 226 -15.8566.770 15.676 1.00 33.19 C C

ATOM 6471CB SERC 226 -16.5756.330 14.402 1.0D 33.61 C C

ATOM 6472OG SERC 226 -16.5307.367 13.435 1.00 37.36 C O

ATOM 6473C SERC 226 -15.5055.553 16.505 1.00 32.03 C C

ATOM 6474O SERC 226 -14.8234.650 16.011 1.00 31.02 C O

ATOM 6475N SERC 227 -15.9745.538 17.756 1.00 31.42 C N

ATOM 6476CA SERC 227 -15.7234.424 18.679 1.00 31.52 C C

ATOM 6477CB SERC 227 -16.6343.245 18.332 1.00 32.26 C C

ATOM 6478OG SERC 227 -17.9833.670 18.236 1.00 35.68 C 0 ATOM 6479C SERC 227 -14,2763.970 18.593 1.00 30.29 C C

ATOM 6480O SERC 227 -14,0012.771 18.504 1.00 29.76 C O

ATOM 6481N VALC 228 -13.359. 4.93718.614 1.00 30.83 C N
' ATOM 6482CA VALC 228 -11.9274.666 18.518 1.00 28,91 C C

ATOM 8483CB VALC 228 -11.0875.928 18.843 1.00 29.89 C C

ATOM 6484CG1VALC 228 -9.636 5.687 18.457 1.0D 26.86 C C

ATOM 6485CG2VALC 228-11.6657.158 18.134 1.00 27.95 C C

ATOM 6486C VALC 228-11-4913.554 19.461 1.00 29.31 C C

ATOM 6487O VALC 228-10.9562.526 19.024 1.00 28.55 C O

ATOM 6488N LEUC 229-11.7153.748 20.757 1,00 30.07 C N

ATOM 6489CA LEUC 229-11.3052.728 21.717 1..0031.94 C C

ATOM 6490CB LEUC 229-11.5333.227 23.151 1.00 31.76 C C

ATOM 6491CG LEUC 229-10.5224.292 23.5 1.00 31.74 C C

ATOM 6492CD1LEUC 229-10.8044.709 __ 1,00 31.11 C C
_ 25.032 ATOM 6493CD2LEUC 229-9.100 3.743 23.476 1.00 32.31 C C

ATOM 6494C LEUC 229-11.9761.361 21.501 1.00 31 C C
.64 ATOM 6495O LEUC 229-11.2910.333 21.477 1.00 _ C O
_ 30.63 ATOM 6496N GLUC 230-13.2981.352 21.318 1.00 32.51_G N

ATOM 6497CA GLUC 230-14.0430.096 21.120 1.00 34.15 C C

ATOM 6498CB GLUC 230-15.5320.379 20.941 1.00 35.31 C C

ATOM 6499CG GLUC 230-16.2050.990 22.170 1.00 36.82 C C

ATOM 6500CD GLUC 230-15.6152,333 22.575 1.0D 38.08 C C

ATOM 6501OE1GLUC 230-15.2043.109 21.683 1.00 40.29 C O

ATOM 6502OE2GLUC 230-15.5782.625 23.789 1.00 39.54 C 0 ATOM _65_03C GLUC 230-13.546-0.71719,928 1.00 35.26 C C

ATOM 6504O GLUC 230-13.435-1.94120.007 1.00 35.53 C O

ATOM 6505N ASNC 231-13.258-0.02918.823 1.00 34.81 C N

ATOM 6506CA ASNC 231-12.747-0.67117.618 1.00 34.09 C C

ATOM 6507CB ASNC 231-12.6440.359 16.476 1.00 34.76 C C

ATOM 6508CG ASNC 231-13.9740.583 15.757 1,00 35.49 C C

ATOM 6509OD7ASNC 231-14.566-0.35915.236 1.00 36.91 C O

ATOM 6510ND2ASNC 231-14.4401.829 15.720 1.00 35.70 C N

ATOM 6511C ASNC 231-11.370-1.24917. 1.00 33.66 C C

ATOM 6512O ASNC 231-11.033-2.376_ 1.00 34.78 C O

17.556 ATOM 6513N HISC 232-10.571-0.47118.656 1.00 32.88 C N

ATOM 6514CA HISC 232-9.239 -0.916___19.0271.00 31.06 C C

ATOM 6515CB HISC 232-8.464 0.228 19.693 1.00 29.12 C C

ATOM 6516CG HISC 232-7.074 -0,14220.094 1.00 27.48 C C

ATOM 6517CD2HISC 232-6.458 -0 21.300 1.00 28.45 C C
.132 ATOM 6518ND1HISC 232-6.140 _ 19.193 1.00 28.03 C N
-0.605 ATOM 6519CE1HISC 232-5.009 -0.86519.826 1.00 28.25 C C

ATOM 6520NE2HISC 232-5.175 -0,58621-107 1.00 28.42 C N

ATOM 6521C HISC 232-9.310 -2.12119.968 1.00 29.68 C C

ATOM 6522O HISC 232-8.496 -3.04019.859 1.00 30.05 C O

ATOM 6523N HISC 233-10.271-2.11920.892 1.00.29.54 C N

ATOM 6524CA HISC 233-10.410$.245 21.832 1,00 29.76 C C

ATOM 6525CB HISC 233-11.530-2.99522.850 1.00 27.95 C C

ATOM 6526CG HISC 233-11.296-1,81123.731 1.00 29.13 C C

ATOM 6527CD2HISC 233-12.150-0,87224.202 1.00 27.14 C C

ATOM 6528ND1HISC 233-1_0.0_58_-1.51224.267 1.00 29.40 C N

ATOM 6529CE7HISC 233-10.164-0.44125.032 1.00 29.01 C C

ATOM 6530NE2HISC 233-11.422-0.03525.010 1.00 29.46 C N

ATOM 6531C HISC 233-10.708-4.53421.075 1.00 30.03 C C

ATOM 6532O HISC 233-10.083-5.56321.319 1.00 31.08 C O

ATOM 6533N LEUC 234-11.671-4.47920.164 1.00 30.87 C N

ATOM 6534CA LEUC 234-12.009-5.64919.355 1.00 32.62 C C

ATOM 6535CB LEUC 234-13.093-5.31018.335 1.00 32.61 C C

ATOM 6536CG LEUC 234-14.507-5.08518.833 1.00 32.90 C -C

ATOM 6537CD1LEUC 234-15.352-4.50317.705 1.00 33.99 C C

ATOM 6538CD2LEUC 234-15.078-8.42319.322 1.00 33.21 C C

ATOM 6539C LEUC 234-10.774-6.07218.589 1.00 33.35 C C

ATOM 6540O LEUC 234-10.409-7,24218.587 1.00 34.53 C O

ATOM 6541N ALAC 235-10.135-5.10117.940 1.00 33.19 C N

ATOM 6542CA ALAC 235-8.949 -5.36317.138 1.00 33.64 C C

ATOM 6543CB ALAC 235-8.412 -4.04316.546 1.00 32.88 C C

ATOM 6544C ALAC 235-7.847 -6,09517.893 1.00 33.80 C C

ATOM 6545O ALAC 235-7.322 -7.09517.413 1.00 34.70 C O

ATOM 6546N VALC 236-7.485 -5.61319.075 1.00 35.27 C N

ATOM 6547CA VALC 236-6.424 -6.27919.834 1.00 35.53 C C

ATOM 6548CB VALC 2365.949 -5.41921.006 1.00 35.09 C C

ATOM 6549CGiVALC 236-4.867 -6.16921.796 1.00 33.83 C C

ATOM 6550CG2VALC 236-5.421 -4.09020.476 1.00 34.90 C C

ATOM 6551C VALC 236-6.874 -7.63020.377 1.00 36.39 C C

ATOM 6552O VALC 236-6.091 -8.58720.414 1.00 35.74 C O
ATOM 6553N GLYC 237-8.136 -7.69220.799 1.00 36.47 C N
ATOM 6554CA GLYC 237-8.686 -8.92121.331 1.00 37.39 C C

ATOM 6555C GLYC 237-8.554 -10.07320.352 1.00 37.79 C C

ATOM 6556O GLYC 237-8.108 -11,14820.734 1.00 36.59 C O
ATOM 6557N PHEC 238-8.944 -9.846(9.098 1.00 39.02 C N

ATOM 6558CA PHEC 238-8.864 -10.86818.054 1.00 40.77 C C

ATOM 6559CB PHEC 238-9.624 -10.43816.794 1.00 39.72 C C

ATOM 6560CG PHEC 238-11.125-10,41016.949 1,00 42.00 C C

ATOM 6561CD1PHEC 238-11.819-11.52617.414 1.00 41.69 C C

ATOM 6562CD2PHEC 238-11.854-9.28016.579 1.00 41.71 C C

ATOM 6563CE1PHEC 238-13.223-11.51717.506 1.00 41.74 C C

ATOM 6564CE2PHEC 238-13.257-9.26316.668 1,00 42.16 C C

ATOM 6565CZ PHEC 238-13.940-10.38717.133 1.00 40.68 C C

ATOM 6566C PHEC 238-7.417 -11.13217.658 1.00 42.00 C C

ATOM 65670 PHEC 238-6.952 -12,27917,655 1.00 40.51 C O

ATOM 6568N LYSC 239-6.711 -10.05617.323 1.00 43 C N

ATOM 6569CA LYSC 239-5.325 -10.15516.896 1.00 . C C
44.36 ATOM 6570CB LYSC 239-4.711 -8.75316.775 1.00 46.70 C C

ATOM6571CG LYSC 239-3.332 -8.72816.111 1.00 48.69 C C

ATOM6572CD LYSC 239-3.389 -9.13214.636 1.00 50.96 C C

ATOM6573CE LYSC 239-1.990 -9.161__ 14.0171.00 52.37 C C

ATOM6574NZ LYSC 239-2.025 -9.31012.530 1.00 54.61 C N

ATOM6575C LYSC 239-4.493 -11.01617.843 1.00 43.88 C C

ATOM6576O LYSC 239x.581 -11.725- 17.4161.00 44.49 C O

ATOM6577N LEUC 240-4.807 -10.96219.130 1.00 42.98 C N

ATOM6578CA LEUC 240-4.069 -11.75320.098 1.00 42.69 C C

ATOM6579CB LEUC 240-4.420 -11.31121.524 1.00 42.77 C C

ATOM6580CG LEUC 240-3.947 -9.90021.899 1.00 42.18 C C

ATOM6581CDtLEUC 240-4.216 -9.64423.376 1.00 41.19 C C

ATOM6582CD2LEUC 240-2.450 -9.76029.606 1.00 41.05 C C

ATOM6583C LEUC 240-4.306 -13.25519.930 1.00 43.28 C C

ATOM6584O LEUC 240-3.515 -14.06620.416 1.00 42.13 C O

ATOM6585N LEUC 241-5.390 -13.62619.248 1.00 43.44 C N

ATOM6586CA LEUC 241-5.690 -15.03819.013 1.00 44.73 C C

ATOM6587CB LEUC 241-7.039 -15.19018.290 1.00 43.58 C C

ATOM6588CG LEUC 241-8.283 -14.83119.115 1.00 43.39 C C

ATOM6589CD1LEUC 241-9.509 -14.65718.226 1.00 40.08 C C

ATOM6590CD2LEUC 241-8.496 -15.91720.163 1.00 43.18 C C

ATOM6591C LEUC 241-4.584 -15.63518.150 1.00 46.00 C C

ATOM6592O LEUC 241-4.166 -16.78318.339 1.00 45.74 C O

ATOM6593N GLNC 242-4.098 -14.82417.218 1.00 47.73 C N

ATOM6594CA GLNC 242-3.063 -15.23916.285 1.00 49.28 C C

ATOM6595CB GLNC 242-3.014 -14.25415.125 1.00 49.62 C C

ATOM6596CG GLNC 242-4.310 -14.23114.335 1.00 52.09 C C
I

ATOM6597CD GLNC 242-4.339 -13.13613.298 1.00 53.18 C C

ATOM6598OE1GLNC 242-3.388 -12.96612.538 1.00 56.76 C O

ATOM6599NE2GLNC 242-5.436 -12.39013.252 1.00 53.43 C N

ATOM6600C GLNC 242-1.670 -15.42916.862 1.00 50.08 C C

ATOM6601O GLNC 242-0.729 -15.67216.114 1.00 51.12 C O

ATOM6602N GLUC 243-1.523 -15.32918.178 1.00 50.08 C N

ATOM6603CA GLUC 243-0.201 -15.52018.773 1.00 51.19 C C

ATOM6604CB GLUC 243-0.044 -14.68120.052 1.00 50.29 C C

ATOM6605CG GLUC 2430.267 -13.21719.759 1.00 50.67 C C

ATOM6606CD GLUC 2430.931 -12.48520.921 1.00 50.90 C C

ATOM6607OE1GLUC 2431.817 -13.06721.576 1.00 52.73 C O

ATOM6608OE2GLUC 2430.582 -11.31621.168 1.00 50.62 C O

ATOM6609C GLUC 2430.092 -16.98819.059 1.00 51.46 C C

ATOM6610O GLUC 243-0.822 -17.80219.203 1.00 52.84 C O

ATOM6611N GLUC 2441.374 -17.32119.136 1.00 51.87 C N

ATOM6612CA GLUC 2441.802 -18.69419.377 1.00 52.09 C C

ATOM6613CB GLUC 2443.268 -18.71719.809 1. 53.86 C C

ATOM6614CG GLUC 2443.873 -20.11319.848 1.00 55.36 C C

ATOM6615CD GLUC 2443.553 -20.91318.593 1.00 56.62 C C

ATOM6616OE1GLUC 2443.657 -20.34717.475 1.00 54.97 C O

ATOM6617OE2GLUC 2443.204 -22.10918.728 1.00 57.38 C O

ATOM6618C GLUC 2440.959 -19.43220.407 1.00 52.29 C C

ATOM6619O GLUC 2440.921 -19.05121.581 1.00 51.40 C O

ATOM6620N ASNC 2450.290 -20.49319.950 1.00 52.03 C N

ATOM6621CA ASNC 245-0.562 -21.33420.794 1.00 51.32 C C

ATOM6622CB ASNC 2450.302 -22.11121.795 1.00 50.84 C C

ATOM6623CG ASNC 245-0.447 -23.26322.456 1.00 50.78 C C

ATOM6624OD1ASNC 2450.021 -23.84023.445 1.00 49.07 C O

ATOM6625ND2ASNC 245-1.607 -23.61121.907 1.00 49.40 C N

ATOM6626C ASNC 245-1.621 -20.51921.546 1.00 51.85 C C

ATOM6627O ASNC 245-1.868 -20.75122.735 1.00 50.97 C O

ATOM6628N CYSC 246-2.246 -19.57120.850 1.00 52.04 C N

ATOM6629CA CYSC 246-3.267 -18.72421.467 1.00 53.37 C C

ATOM6630CB CYSC 246-2.867 -17.24121.394 1.00 52.82 C C

ATOM6631SG CYSC 246-1.562 -16.74722.548 1.00 55.04 C S

ATOM6632C CYSC 246-4.662 -18.86820.886 1.00 53.39 C C

ATOM6633O CYSC 246-5.634 -18.47321.525 1.00 53.70 C O

ATOM6634N ASPC 247-4.780 ~-19.42119.685 1.00 53.74 C N

ATOM6635CA ASPC 247-6.100 -19.55519.085 1.00 55.28 C C

ATOM6636CB ASPC 247-5.985 -19.99817.625 1.00 55.05 C C

ATOM6637CG ASPC 247-7.266 -19.75116.839 1.00 56.24 C C

ATOM6638OD1ASPC 247-8.209 -19.13217.399 1.00 54.36 C O

ATOM6639OD2ASPC 247-7.321 -20.17015.656 1.00 56.05 C O

ATOM6640C ASPC 247-6.966 -20.54019.878 1.00 56.23 C C

ATOM6641O ASPC 247-6.850 -21.75919.731 1.00 56.93 C O

ATOM6642N ILEC 248-7.829 -19.99820.729 1.00 56.16 C N

ATOM6643CA ILEC 248-8.706 -20.82021.546 1.00 55.77 C C

ATOM6644CB ILEC 248-9.189 -20.04922.801 1.00 53.68 C C

ATOM6645CG2ILEC 248-7.998 -19.68923.679 1.00 53.72 C C

ATOM6646CG1ILEC 248-9.953 -18.79522.383 1.00 51,32 C C

ATOM6647CDtILEC 248-10.416-17.96423.538 1.00 49.89 C C

ATOM6648C ILEC 248-9.915 -21.26620.735 1.00 56.81 C C

ATOM6649O ILEC 248-10.800-21.95321.249 1.00 56.89 C O

ATOM6650N PHEC 249-9.952 -20.87419.467 1.00 57.46 C N

ATOM6651CA PHEC 249-11.064-21.25118.606 1.00 58.85 C C

ATOM6652CB PHEC 249-11.788-20.00018.101 1.00 58.51 C C

ATOM6653CG PHEC 249-12.181-19.03819.195 1.00 59.14 C C

ATOM6654CD1PHEC 249-12.857-19.48420.330 1.00 58.64 C C
ATOM6655CD2PHEC 249-11.899-17.67619.077 1.00 58.84 C C

ATOM6656CE1PHEC 249-13.249-18.58821.331 1.00 58.75 C C

ATOM6657CE2PHE C 249-12.286-16.77020.073 1.00 58.95 C C

ATOM6658CZ PHE C 249-12.963-17.22829.202 1.00 58.39 C C

ATOM6659C PHE C 249-10.537-22.06617.430 1.00 60.05 C C

ATOM6660O PHE C 249-11.207-22.21916.408 1:00 59.95 C O

ATOM6661N GLN C 250-9.326 -22.59317.590 1.00 61.75 C N

ATOM6662CA GLN C 250-8.688 -23.38716.547 1.00 62.50 C C

ATOM6663CB GLN C 250-7.319 -23.87717.024 1.00 62.25 C C

ATOM6664CG GLN C 250-7.374 -24.80918.218 1.00 61.73 C C

ATOM6665CD GLN C 250-6.000 -25.14018.752 1.00 62.37 C C

ATOM6666OE1GLN C 250-5.274 -24.25819.215 1.00 63.57 C O

ATOM6667NE2GLN C 250-5.629 -26.41318.691 1.00 61.92 C N

ATOM6668C GLN C 250-9.540 -24.58316.133 1.00 63.17 C C

ATOM6669O GLN C 250-9.528 -24.98314.970 1.00 63.26 C O

ATOM6670N ASN C 251-10.281-25.15017.082 1.00 63.62 C N

ATOM6671CA ASN C 251-11.115-26.30616.782 1.00 64.15 C C

ATOM6672CB ASN C 251-11.010-27.35017.898 1.00 63.55 C C

ATOM6673CG ASN C 251-9.700 -28.11217.850 1.00 62.86 C C

ATOM6674OD1ASN C 251-9.229 -28.47616.774 1.00 62.09 C O

ATOM6675ND2ASN C 251-9.112_-28.36719.014 1.00 62.58 C N

ATOM6676C ASN C 251-12.577-26.00216.493 1.00 64.44 C C

ATOM6677O ASN C 251-13.376-26.92016.344 1.00 64.44 C O

ATOM6678N LEU C 252-12.936-24.72416.421 1.00 65.23 C N

ATOM6679CA LEU C 252-14.310-24.36916.091 1.00 66.37 C C

ATOM6680CB LEU C 252-14.600-22.88916.358 1.00 66.69 C C

ATOM6681CG LEU C 252-14.500-22.27617.752 1.00 67.29 C C

ATOM6682CD1LEU C 252-15.033-20.84817.698 1.00 67.90 C C

ATOM6683CD2LEU C 252-15.299-23.08918.742 1.00 68.02 C C

ATOM6684C LEU C 252-14.409-24.60514.592 1.00 67.25 C C

ATOM6685O LEU C 252-13.428-24.99313.956 1.00 67.85 C O

ATOM6686N THR C 253-15.582-24.36714.021 1.00 67.59 C N

ATOM6687CA THR C 253-15.748-24.54412.587 1.00 67.90 C C

ATOM6688CB THR C 253-16.997-25.38812.247 1.00 67.27 C C

ATOM6689OG1THR C 253-18.152-24.81612.875 1.00 66.08 C O

ATOM6690CG2THR C 253-16.810-26.52512.714 1.00 66.71 C C

ATOM6691C THR C 253-15.892-23.17711.941 1.00 68.48 C C

ATOM6692O THR C 253-16.188-22.19012.617 1.00 68.12 C O

ATOM6693N LYS C 254-15.677-23.12210.633 1.00 68.74 C N

ATOM6694CA LYS C 254-15.796-21.8699.910 1.00 69.23 C C

ATOM6695CB LYS C 254-15.663-22.1148.402 1.0D 69.93 C C

ATOM6696CG LYS C 254-15.651-20.8487.563 1.00 71.62 C C

ATOM6697CD LYS C 254-14.470-19.9627.940 1.00 74.19 C C

ATOM6698CE LYS C 254-14.500-18.6287.202 1.00 74.65 C C

ATOM6699NZ LYS C 254-13.358-17.7517.600 1.00 74.51 C N

ATOM6700C LYS C 254-17.148-21.23110.225 1.00 68.75 C C

ATOM67010 LYS C 254-17.221-20.05110.560 1.00 69.27 C O

ATOM6702N LYS C 255-18.214-22.01810.134 1.00 68.09 C N

ATOM6703CA LYS C 255-19.557-21.51010.400 1.00 67.69 C C

ATOM6704CB LYS C 255-20.592-22.62710.213 1.00 68.56 C C

ATOM6705CG LYS C 255-22.032-22.23910.560 1.00 69.29 C C

ATOM6706CD LYS C 255-22.512-21.0329.766 1.00 69.55 C C

ATOM6707CE LYS C 255-23:961-20.69510.097 1.00 69.63 C C

ATOM6708NZ LYS C 255-24.401-19.4369.433 1.00 68.78 C N

ATOM6709C LYS C 255-19.666-20.92811.803 1.00 66.64 C C

ATOM67100 LYS C 255-20.417-19.97812.031 1.00 66.14 C O

ATOM6711N GLN C 256-18.912-21.50112.736 1.00 65.55 C N

ATOM6712CA GLN C 256-18.917-21.04414.120 1.00 65.66 C C

ATOM6713CB GLN C 256-18.440-22.16515.049 1.00 66.46 C C

ATOM6714CG GLN C 256-19.427-23.31515.183 1.00 66.97 C C

ATOM6715CD GLN C 256-18.947-24.38416.146 1.00 67.67 C C

ATOM6716OE1GLN C 256-17.902-25.00315.931 1.00 68.24 C O

ATOM6717NE2GLN C 256-19.709-24.60717.216 1.00 66.99 C N

ATOM6718C GLN C 256-18.051-19.79914.320 1.00 64.97 C C

ATOM6719O GLN C 256-18.543-18.76914.784 1.00 65.29 C O

ATOM6720N ARG C 257-16.768-19.90013.972 1.00 63.63 C N

ATOM6721CA ARG C 257-15.842-18.77914.106 1.00 62.16 C C

ATOM6722CB ARG C 257-14.522-19.08413.390 1.00 62.08 C C

ATOM6723CG ARG C 257-13.663-20.09814.126 1.00 63.36 C C

ATOM6724CD ARG C 257-12.270-20.22613.537 1.00 64.98 C C

ATOM6725NE ARG C 257-12.141-21.38012.651 1.00 66.81 C N

ATOM6726CZ ARG C 257-12.473-21.39111.363 1.00 67.59 C C

ATOM6727NH1ARG C 257-12.959-20.29990.780 1.00 67.47 C N

ATOM6728NH2ARG C 257-12.323-22.50610.657 1.00 68,27 C N

ATOM6729C ARG C 257-16.461-17.51713.531 1.00 61.38 C C

ATOM6730O ARG C 257-16.425-16.45114.146 1.00 61.35 C O

ATOM6731N GLN C 258-17.052-17.65012.354 1.00 60.06 C N

ATOM6732CA GLN C 258-17.676-16.52211.695 1,00 58.83 C C

ATOM6733CB GLN C 258-18.166-16.94310.307 1.00 60.45 C C

ATOM6734CG GLN C 258-18.773-15.8139.488 1.00 62.42 C C

ATOM6735CD GLN C 258-18.977-16.1928.032 1.00 64.29 C C

ATOM6736OE1GLN C 258-18.016-16.4907.314 1.00 64.57 C 0 ATOM6737NE2GLN C 258-20.233-16.1857.588 1.0D 64.51 C N

ATOM6738C GLN C 258-18.829-15.96612.522 1.00 57.62 C C

ATOM6739O GLN C 258-18.973-14.75112.658 1.00 57.02 C O

ATOM6740N SER C 259-19.647-16.85413.084 1.00 56.73 C N

ATOM6741CA SER C 259-20.787-16.41313.886 1.00 55.31 C C

ATOM6742CB SER C 259-21.724-17.58814.184 1.00 55.99 C C

ATOM6743OG SERC 259-22.942-17.12414.755 1.00 57.10 C 0 ATOM6744C SERC 259-20.318-15.76815.189 1.00 53.22 C C

ATOM6745O SERC 259-20.836-14.72915.604 1.00 52.01 C O

ATOM6746N LEUC 260-19.335-16.39215.828 1.00 51.92 C N

ATOM6747CA LEUC 260-18.774-15.87117.069 1.00 50.95 C C

ATOM6748CB LEUC 260-17.660-16.79217.569 1.00 50.90 C C

ATOM6749CG LEUC 260-16.943-16.37218.851 1.00 51.64 C C

ATOM6750CD1LEUC 260-17.921-16.42820.007 1.00 51.42 C C

ATOM6751CD2LEUC 260-15.745-17.28619.109 1.00 51.84 C C

ATOM6752C LEUC 260-18.212-14.47716.786 1.00 50.36 C C

ATOM6753O LEUC 260-18.538-13.51817.485 1.00 50.34 C O

ATOM6754N ARGC 261-17.388-14.36415.745 1.00 49.46 C N

ATOM6755CA ARGC 261-16.800-13.07715.388 1.00 48.53 C C

ATOM6756CB ARGC 261-16.027-13.13714.057 1.00 48.44 C C

ATOM6757CG ARGC 261-15.541-11_.74813.609 1.00 48.46 C C
i ATOM6758CD ARGC 261-14.796-11.71912.276 1.00 50.21 C C
, ATOM6759NE ARGC 261-14.548-10.33819.838 1.00 50.47 C N
I

ATOM6760CZ ARGC 261-13.714-9.45912.445 1.00 50.39 C C
, ATOM6761NH1ARGC 261-13.031-9.87513.519 1.00 49.87 C N

ATOM6762NH2ARGC 26i-13.573-8.24511.993 1.00 48.82 C N

ATOM6763C ARGC 261-17.857-11.99415.286 1.00 47.48 C C

ATOM6764O ARGC 261-17.753-10.96715.951 1.00 48.34 C O

ATOM6765N LYSC 262-18.875-12,21114.463 1.00 46.26 C N

ATOM6766CA LYSC 262-19.909-11.19914.310 1.00 45.47 C C

ATOM6767CB LYSC 262-21.000-11.66013.341 1.00 46.44 C C

ATOM6768CG LYSC 262-22.244-10.76713.405 1.00 47.38 C C

ATOM6769CD LYSC 262-22.870-10.50412.049 1.00 47:52 C C

ATOM6770CE LYSC 262-23.878-9.36612.156 1.00 48.12 C C

ATOM6771NZ LYSC 262-24.258-8.82110.821 1.00 49.60 C N

ATOM6772C LYSC 262-20.563-10.77415.610 1.00 45.32 C C

ATOM6773O LYSC 262-20.859-9.59415.794 1.00 45.69 C O

ATOM6774N METC 263-20.801-11.72516.509 1.00 45.73 C N

ATOM6775CA METC 263-21.453-11.40317.777 1.00 45.92 C C

ATOM6776CB METC 263-21.943-12.68218.478 1.00 46.89 C C

ATOM6777CG METC 263-23.073-13.39917.741 1.00 48.63 C C

ATOM6778SD METC 263-23.806-14.79518.643 1.00 48.44 C S

ATOM6779CE METC 263-22.549-16.04618.442 1.00 44.52 C C

ATOM6780C METC 263-20.561-10.59718.717 1.0D 44.54 C C

ATOM6781O METC 263-21.025-9.64519.351 1.00 43.70 C O

ATOM6782N VALC 264-19.288-10.96918.811 1.00 43.82 C N

ATOM6783CA VALC 264-18.377-10.23819.681 1.00 44.71 C C

ATOM6784CB VALC 264-16.984-10.89919.716 1.00 45.19 C C

ATOM6785CG1VALC 264-16.001-10.02020.473 1.00 45.22 C C

ATOM6786CG2VALC 264-17.081-12.25020.410 1.00 45.41 C C

ATOM6787C VALC 264-18.270-8.78619.214 1.00 44.49 C C

ATOM6788O VALC 264-18.351-7.86220.017 1.00 43.30 C O

ATOM6789N ILEC 265-18.111-8.58517.910 1.00 45.49 C N

ATOM6790CA ILEC 265-18.024-7.23417.365 1.00 45.09 C C

ATOM6791CB ILEC 265-17.992-7.23815.816 1.00 43.82 C C

ATOM6792CG2ILEC 265-18.261-5.83715.282 1.00 43.46 C C

ATOM6793CG1ILEC 265-16.650-7.76595.317 1.00 44.00 C C

ATOM6794CD1ILEC 265-16.507-7.73313.800 1.00 42.21 C C

ATOM6795C ILEC 265-19.252-6.44117.796 1.00 45.57 C C

ATOM6796O ILEC 265-19.151-5.30918.264 1.00 46.72 C 0 ATOM6797N ASPC 266-20.418-7.04717.629 1.00 45.63 C N

ATOM6798CA ASPC 266-21.664-6.38517.972 1.00 46.39 C C

ATOM6799CB ASPC 266-22.850-7.26117.560 1.00 48.51 C C

ATOM6800CG ASPC 266-23.072-7.26816.061 1.00 49.82 C C

ATOM6801OD1ASPC 266-23.842-8.12415.573 1.00 50.58 C O

ATOM6802OD2ASPC 266-22.479-6.40615.371 1.00 51.00 C 0 ATOM6503C ASPC 266-21.770-6.03719.441 1.00 45.59 C C

ATOM6804O ASPC 266-22.212-4.94619.795 1.00 45.90 C O

ATOM6805N ILEC 267-21.362-6.963_20_299_1.00 44.36 C N

ATOM6806CA ILEC 267-21.443-6.72721.731 _1.00 _43_.01C C

ATOM6807CB ILEC 267-21.169-8.04522.523 1.00 42.62 C C

ATOM6808CG2ILEC 267-20.913-7.74923.997 1.00 41.75 C C

ATOM6809CG1ILEC 267-22.373-8.98422.378 1.0D 41.72 C C

ATOM6810CD1ILEC 267-22.125-10.38022.867 1.00 41.12 C C

ATOM6811C ILEC 267-20.487-5.62322.169 1.00 42.54 C C

ATOM6812O ILEC 267-20.919-4.62122.736 1.00 41.83 C O

ATOM6813N VALC 268-19.196-5.79621.887 1.00 42.10 C N

ATOM6814CA VALC 268-18.194-4.80922.283 1.00 41.75 C C
ATOM6815CB VALC 268-16.783-5.21621.830 1.00 41.57 C C

ATOM6816CG1VALC 268-15.768-4.16222.266 1.00 42.91 C C

ATOM6817CG2VALC 268-16.418-6.55722.416 1.00 41.52 C C

ATOM6818C VALC 268-18.479-3.40821.762 1.00 41.39 C C
ATOM6819O VALC 268-18.379-2.43722.510 1.00 40.47 C O
ATOM6820N LEUC 269-18.837-3.28720.488 1.00 41.63 C N

ATOM6821CA LEUC 269-19.114-1.96319.950 1.00 41.61 C C

ATOM6822CB LEUC 269-19.449-2.02718.462 1.00 41.19 C C

ATOM6823CG LEUC 269-18.244-2.15917.525 1.00 41.69 C C

ATOM6824CD1LEUC 269-18.717-2.33216.092 1.00 39.96 C C

ATOM6825CD2LEUC 269-17.370-0 17.646 1.00 42 C C
.923 .05 ATOM6826C LEUC 269-20.249_ 20.712 1.00 _ C C
_ 41.77 1.320 ATOM6827O LEUC 269-20.360-0.09520.761 1.00 42.64 C O

ATOM6828N ALAC 270-21.086-2.14021.332 1.00 42.19 C N

ATOM 829 A LA C 70 -22.207-1.59922.091 1.00 42.48 C
6 C A LA 2 70 -23.259-2.68322.316 1.00 43.01 C C
ATOM 830 B LA C 70 -21.786-0.97623.428 1.00 41.53 C
6 C A ALA 2 270-22.538-0.19524.000 1.00 41.49 C O
ATOM 6831C C 2 23 1.00 41.58 C N

O C C

ATOM 6833N THR C 271-20.589-1.30 . 1.00 41.55 C C
ATOM 6834CA THR C 271-20.105-0.75525.191 1.00 41.04 C C
ATOM 6835CB THR C 271-18,864-1.49925.712 1.00 39.49 C O
ATOM 6836OG1THR C 271-17.771-1.28224.814 1.00 40.77 C C
ATOM 6837CG2THR C 271-19.13$-2.9$725.838 1.00 42.36 C C
ATOM 6838C THR C 271-19.7300.721 25.116 1.00 41.51 C O
ATOM 6839O THR C 271-19.4051.332 26.135 1.00 44.16 C N
ATOM 6840N ~ C 272-19.7541.277 23.908 1.00 45.87 C C
ATOM 6841CA ASP C 272-19.4252.687 23.685 1.00 45.58 C C
ATOM 6842CB ASP C 272-19.2512.949 22.182 1.00 45.40 C C
ATOM 6843CG ASP C 272-18.8264.384 21.863 1.00 44.74 C O
ATOM 6844OD1ASP C 272-19.0025.303 22.702 1.00 44.85 C O
ATOM 6845OD2ASP C 272-18.3254.591 20.740 1.00 48.21 C C
ATOM 6846C ASP C 272-20.5843.514 24.217 1.00 46.34 C O
ATOM 6847O ASP C 272-21.6903.427 23.700 1.00 48.05 C N
ATOM 6848N ASP C 273-20.3264.321 25.239 1.00 50.20 C C
ATOM 6849CA MET C 273-21.3705.146 25.849 1.00 50.12 C C

ATOM 6850CB MET C 273-20.7755. . 1.00 51.87 C C
ATOM 6851CG MET C 273-20.4185.192 28.208 1.00 54.39 C S
ATOM 6852SD MET C 273-2t.8484.295 28.887 1.00 50.93 C C
ATOM 6853CE MET C 273-22.9285.661 29.385 1.00 51.30 C C
ATOM 6854C MET C 273-22.1936.041 24.914 1.0D 51.78 C 0 ATOM 6855O MET C 273-23.318. . 1.00 52.14 C N
ATOM 6856N SER C 274-21.6516.382 23.748 1.00 51.88 C C
ATOM 6857CA SER C 274-22.3937.224 22.810 1.00 51.84 C C
ATOM 6$58CB SER C 274-21.4777.709 21.678 1.00 50.10 C O
ATOM 6859OG SER C 274-21.1166.649 20.807 1.00 52.57 C C
ATOM 6860C SER C 274-23.5566:416 22.228 1.00 52.08 C O
ATOM 6861O SER C 274-24.4296.962 21,551 1.00 53.20 C N
ATOM 6862N LYS C 275-23.5605.113 22.504 1.00 54.58 C C

ATOM 6863CA LYS C 275-24.605. . 1.00 54.36 C C
ATOM 6864CB LYS C 275-23.9852.904 21.520 1.00 55.57 C C
ATOM 6865CG LYS C 275-22.9163.051 20.451 1.00 55.60 C C

ATOM 6866CD LYS C 275-23.503. . 1.00 55.84 C C
ATOM 6867CE LYS C 275-22.4493.266 18,022 1.00 57.90 C N
ATOM 6868NZ LYS C 275-23.0543.215 16.664 1.00 55.44 C C
ATOM 6869C LYS C 275-25.6133.886 23.122 1.00 55.10 C O
ATOM 6870O LYS C 275-26.6583.281 22.868 1.00 56.62 C N
ATOM 6871N HIS C 276-25.2784.277 24.348 1.00 57.88 C C
ATOM 6872CA HIS C 276-26.1204.026 25.512 1.00 57.73 C C
ATOM 6873CB HIS C 276-25.5644.777 26.725 1.00 58.17 C C
ATOM 6874CG HIS C 276-26.4654.742 27.920 1.00 58.02 C C
ATOM 6875CD2HIS C 276-27.1695.723 28.532 1.00 57.53 C N
ATOM 6876ND1HIS C 276-26.7403.582 28.612 1.00 58.11 C C
ATOM 6877CE1HIS C 276-27.5763.852 29.599 1.00 57.65 C N
ATOM 6878NE2HIS C 276-27.8525.143 29.573 1.00 59.17 C C
ATOM 6879C HIS C 276-27.5894,403 25.312 1.00 5$.25 C O
ATOM 6880O HIS C 276-28.4663.537 25.338 1.00 60.31 C N
ATOM 6881N MET C 277-27.8515.694 25.127 1.00 62.60 C C
ATOM 6882CA MET C 277-29.2136.176 24.937 1.00 63.28 C C
ATOM 6883CB MET C 277-29.2057.634 24.474 1.00 64.83 C C
ATOM 68$4CG MET C 277-28.7078.613 25.527 1.00 67.35 C S
ATOM 6885SD MET C 277-29.5538.384 27.110 1.00 65.64 C C
ATOM 6886CE MET C 277-28.2528.841 28.287 1.00 83.61 C C
ATOM 6887C MET C 27730.0105.328 23.952 1.00 64.15 C O
ATOM 6888O MET C 277-31.1785.018 24.196 1.00 64.40 C N
ATOM 6889N ASN C 278-29-3874.949 22.841 1.00 65.93 C C
ATOM 6890CA ASN C 278-30.0774.132 21.852 1 66 C C

ATOM 6891CB ASN C 278-29.3064.115 20.526 . . C C
ATOM 6892CG ASN C 278-29.4375.425 19.758 1.00 67.01 C O
ATOM 6893OD1ASN C 278-34.5365.984 19.637 1.00 65.65 C N
ATOM 6894ND2ASN C 278-28.31$5.914 19.224 1.00 66.58 C C
ATOM 6895C ASN G 278-30.3052.703 22.342 1.00 66.78 C 0 ATOM 6896O ASN C 278-31.3792.138 22.133 1.00 66.97 C N
RTOM 6897N LEU C 279-29.3002.118 22.990 1.00 67.44 C C
ATOM 6898CA LEU C 279-29.4310.760 23.504 1.00 68.16 C C
ATOM 6899CB LEU C 279-28.1340.307 24.174 1.00 67.46 C C
ATOM 6900CG LEU C 279-27.045-0.24023.254 1.00 67.59 C C
ATOM 6901CD1LEU C 279-25.900-0.76924.101 1.00 67.07 C C
ATOM 6902CD2LEU C 279-27.610-1.35322.385 1.00 66.63 C C
ATOM 6903C LEU C 279-30.5750.655 24.506 1.00 68.90 C O
ATOM 6904O LEU C 27931.327-0.32324.501 1.00 68.66 C N

ATOM 6905N LEU C 280-30.6971.668 25.363 . . C C
ATOM 6906CA LEU C 280-31.7421.703 26.379 1.00 70.55 C C
ATOM 6907CB LEU C 280-31.5262.$84 27.328 1.00 70.04 C C
ATOM 690$CG LEU C 280-32.5252.979 28.488 1.00 69.77 C G
ATOM 6909CDtLEU C 28032.4761.702 29.306 1.00 69.46 C C
ATOM 6910CD2LEU C 280-32.1994.181 29.361 1.00 69.35 C C
ATOM 6911C LEU C 28033.1221.805 25.743 1.00 71.50 C O
ATOM 6912O LEU C 280X4.0491.098 26.141 1.0D 72.21 C N
ATOM 6913N ALA C 28133.2572.692 24.762 1.00 72.23 C C
ATOM 6914CA ALA C 281-34.5242.870 24.067 1.00 72.98 2~~

ATOM6915CB ALA~ 281-34.3733.903 22.967 1.00 72.61 C C
C

ATOM6916C ALAC 281__-34.9741.533 23.479 1.00 73:82 C C

ATOM69170 ALAC 281-36.1231.129 23.645 1.00 74.54 C O

ATOM6918N ASPC 2 - 0.847 22.791 1.00 74.68 C N
8234.067 ATOM6919CA ASPC _ _ -0.44 22.200 _ ___ C C
28234.386 8 1.00 75.83 ATOM6920CB ASPC 282_ _ __ _ __ C C
ATOM6921CG ASPC 282-33.192_ 21.411 1.00 _ _ C C
ATOM6922OD1ASPC 282-33.105-0.99820.011 _1.00 76.19 C O
ATOM6923OD2ASPC 282-34.047-0.42819.221 1.00 __76.5_3C O
-32.095-0.64319.697 1.00 76.70 0.232 77.62 ATOM6924C ASPC 282-34.768-1.44423.284 1.00 76.60 C C

ATOM6925O ASPC 28235.740 -2.18423.140 1.00 76.87 C O

ATOM6926N LEUC 283-33.999-1.46024.370 1.00 77.25 C N

ATOM6927CA LEUC 283-34.265-2.37125.475 _ 77.90 C C
__ 1.00 ATOM6928CB LEUC 283-33.266-2.14526.612 1.00 76.58 C C
ATOM6929CG LEUC 283-33.298-3.22727.692 1.00 75.32 C C

ATOM6930CD1LEUC 28332.907 -4.55627.065 1.00 74.69 C C

ATOM6931CD2LEUC 283-32.357-2.87028.829 1.00 74.43 C C

ATOM6932C LEUC 283-35.684-2.17225.997 1.00 78.94 C C

ATOM6933O LEUC 283-36.403-3.14026.242 1.00 78.90 C O

ATOM6934N LYSC 284-36.080-0.91326.164 1.00 80.14 C N

ATOM6935CA LYSC 284-37.417-0.59026.650 1.00 81.41 C C

ATOM6936CB LYSC 28437.570 0.924 26.828 1.00 79.93 C C

ATOM6937CG LYSC 284-36.6991.511 27.924 1.00 78.24 C C

ATOM6938CD LYSC 284-37.0382.971 28.170 1.00 76.70 C C

ATOM6939CE LYSC 284-36.2413.526 29.334 1.00 76.28 C C

ATOM6940NZ LYSC 284-36.5824.943 29.625 1.00 74.73 C N

ATOM6941C LYSC 284-38.482-1.10325.683 1.00 83.18 C C

ATOM6942O LYSC 28439.451 -1.74026.098 1.00 83.51 C O

ATOM6943N THRC 285-38.294-0.82524.395 1.00 84.86 C N

ATOM6944CA THRC 285-39.235-1.25823.372 1.00 86.34 C C

ATOM6945CB THRC 285-38.789-0.80021.966 1.00 86.53 C C

ATOM6946OGtTHRC 285-38.6000.622 21.959 1.0D 86.15 C O

ATOM6947CG2THRC 28539.842 -1.16920.928 1.00 86.42 C C

ATOM6948C THRC 28539.352 -2.77823.374 1.00 87.61 C C

ATOM6949O THRC 285-40.405-3.32623.055 1.00 87.91 C O

ATOM6950N METC 286X8.264 -3.45223.739 1.00 88.97 C N

ATOM6951CA METC 286X8.243 -4.91123.783 1.00 90.52 C C

ATOM6952CB METC 286-36.799-5.42623.754 1.00 90.54 C C

ATOM6953CG METC 286-36.681-6.94623.727 1.00 90.63 C C

ATOM6954SD METC 286-34.970-7.53623.689 1.00 91.41 C S

ATOM6955CE METC 28634.649 -7.52821.935 1.00 90.71 C C

ATOM6956C METC 286-38.949-5.43525.031 1.00 91.33 C C

ATOM69570 METC 286-39.369-6.59225.077 1.00 91.62 C O

ATOM6958N VALC 2$7-39.073-4.5$026.042 1.00 92.20 C N

ATOM6959CA VALC 287-39.736-4.95827.286 1.00 93.12 C C

ATOM6960CB VALC 287-39.120-4.21328.491 1.00 92.91 C C

ATOM6961CG7VALC 28739.887 -4.53629.762 1.00 92.98 C C

ATOM6962CG2VALC 287-37.666-4.61828.649 1.00 92.81 C C

ATOM6963C VALC 287-41.232-4.65727.204 1.00 93.76 C C

ATOM6964O VALC 287-42.016-5.13328.026 1.00 93.75 C O

ATOM6965N GLUC 288-41.618-3.86926.203 1.00 94.42 C N

ATOM6966CA GLUC 288-43.0173.518 25.994 1.00 95.00 C C

ATOM6967CB GLUC 288-43.148-2.04825.590 1.00 95.64 C C

ATOM6968CG GLUC 288-42.797-1.07326.703 1.00 97.07 C C

ATOM6969CD GLUC 288-43.1220.365 26.344 1.00 98.05 C C

ATOM6970OE1GLUC 288-44.2950.644 26.014 1.00 98.62 C O

ATOM6971OE2GLUC 288-42.2091.219 26.395 1.00 98.65 C O

ATOM6972C GLUC 288-43.603-4.41224.909 1.00 95.05 C C

ATOM6973O GLUC 288-44.620-4.08924.294 1.00 95.04 C O

ATOM6974N THRC 289-42.937-5.53824.683 1.00 95.10 C N

ATOM6975CA THRC 289-43.352-6_.51723.689 1.00 95.68 C C

ATOM6976CB THRC 289-42._78_1-6.18222.297 1.00 95.56 C C

ATOM6977OG1THRC 289-43.094-4.82321.970 1.00 95.11 C O

ATOM6978CG2THRC 289-43.385-7.09921.235 1.00 95.34 C C

ATOM6979C THRC 289-42.798-7.85624.158 1.00 96.38 C C

ATOM69800 THRC 289-42.692-8.81723.395 1.00 96.50 C O

ATOM6981N LYSC 290-42.438-7,89025.435 1.00 97.05 C N

ATOM6982CA LYSC 290-41.891-9.07926.071 1.00 97.70 C C

ATOM6983CB LYSC 290-41.883-$.87027.590 1.00 98.08 C C

ATOM6984CG LYSC 290-41.287-10.00228.410 1.00 98.26 C C

ATOM6985CD LYSC 290-41.291-9.64529 1.00 98.27 C C
.895 ATOM6986CE LYSC 290-_40.6_91-10.760_ 1.00 98.55 C C
_ 30.745 ATOM6987NZ LYSC 290-40.611-10.40232.191 1.00 98.48 C N

ATOM6988C LYSC 290-42.730-10.30025.702 1.00 98.10 C C

ATOM69890 LYSC 290-43.959-10.24725.724 1.00 98.17 C O

ATOM6990N LYSG 291-42.060-11.39225.353 1.00 98.53 C N

ATOM6991CA LYSC 291-42.743-12.62724.983 1.00 99.11 C C

ATOM6992CB LYSC 291-42.586-12.89423. 1.00 99.22 C C

ATOM6993CG LYSC 291-43.069-11.769__ 1.00 99.48 C C
_ 22.591 ATOM6994CD LYSC 291-42.784-12.08521.127 1.00 99.84 C C

ATOM6995CE LYSC 291-43.185-10.93520.211 1.00 99.55 C C

ATOM6996NZ LYSC 291-42.861-11.22418.787 1.00 98.92 C N

ATOM6997C LYSC 291-42.159-13.80125.762 1.0D 99.47 C C

ATOM6998O LYSC 291-40.999-14.16025.572 7.00 99.47 C O

ATOM6999N VALC 292-42.965-14.39726.635 1.00 99.85 C N

ATOM7000CA VALC 292-42.518-15.53327.436 1.00 99.87 C C
~ ~

ATOM 001 B AL 2 92-42.973-15.39028.906 1.00 99.91 C
7 C V C 2 92-42.519-14.04829.459 1.00 C C
ATOM 002 G1 AL 2 92-44.486-15.53329.006 1.00 99.75 C
7 C V C 2 92-43.065-16.84626.873 1.00 C C
ATOM 003 G2 AL 844 913 1.00 99.82 O

ATOM 004 V AL 100,00 100.00 C

ATOM 005 V AL 2 92-43.837. . 1.00 100.00N
7 O T C C 93-42.658- 27.474 1.00 C C
ATOM 006 CA HR 2 93-43.102-17.96327.037 1.00 99.91 C C
7 N CB THRC 93-41.905-19.28726.585 1.00 C C O
ATOM 007 OG1THR2 93-41.081-20.16025,680 1.00 100.00C C
7 008 CG2THRC 293-42,393-19.41425.879 1.00 100.00C C
ATOM 7009C THR2 293-43:807-21.42328.190 1.0D 100.00C O
7 7010O THRC 293-43.926-19.99429.283 1.0D 99.79 G N
ATOM 7011N THR2 294-44.278-19.44227.939 1.00 99.65 C C
ATOM 7012CA SERG 294-44.956-21.21328.966 1.00 100.00C C
ATOM 7013CB SERC 294-45.420-22.00128.384 1.00 100.00C O
ATOM 7014OG SERC 294-46.325-23.34227.309 1.00 100.00C C
ATOM 7015C SERC 294-43.975-23.15130.115 1.00 100.00C O
ATOM 7016O SERC 294-44.373-22.24331.242 1.00 100.00C N
ATOM 7017N SERC 295-42.690-22.56429.806 1.00 100.00C C
ATOM 7018CA SERC 295-41.610-22.07930.769 1.00 100.00C C
ATOM 7019 SERC -22.252051 99.95 ATOM 7020 C 758 30 99.91 ATOM C

ATOM 7029CB SERC 295-40.353. , 1.00 100.00C O
ATOM 7022OG SERC 295-39.276- 30.952 1.00 100.00C C
ATOM 7023C SERC 295-41.323-22.94331.456 1.00 100.00C O
' 7024O SERC 295-40.362-20.91732.214 1.00 100.00C N
ATOM 7025N GLYC 296X2.164 -20.79031,178 1.00 100.00C C
ATOM 7026CA GLYC 296-42.004-19.92231.777 1.00 99.88 C C
ATOM 7027G GLYC 296-40.812-18.60631.254 1.00 99.73 C O
ATOM 7028O GLYC 296-40.772-17.82931.332 1.00 99.81 C N
ATOM 7029N VALC 297-39.836-16.60030.720 1,00 99.72 C C
ATOM 7030CA VALC 297-38.626-18.55230.178 1.00 99.96 C C
ATOM -17.947828 ATOM 7031CB VALC 297-37.579. . 1.00 100.00C C
ATOM 7032CG1VALC 297-36.314- 29.304 1.00 100.00C C
ATOM 7033CG2VALC 297-37.269-18.39231.062 1.00 99.44 C C
ATOM 7034C VALC 297-38.930-19.87928.926 1.00 99.55 C O
ATOM 7035O VALC 297-39.844-17.12228.160 1.00 99.02 C N
-17.445729 ATOM 7036N LEUC 298-38.165. . 1.00 98.55 C C
ATOM 7037CA LEUC 298-38.336-1 27.576 1.00 98.82 C C
ATOM 7038CB LEUC 298-37.291-15.17727.605 1.00 99.24 C C
ATOM 7039CG LEUC 298-37.392-14.06328.727 1.00 99.24 C C
ATOM 7040CD1LEUC 298-36-183-13.03128,681 1.00 99.55 C C
ATOM 7041CD2LEUC 298-38.678-12.10628.572 1.00 98.26 C C
ATOM 7042C LEUC 298-38.206-12.23926.266 1.00 98.21 C O
-15.94526.225 ATOM 7043O LEUC 298-37.637. 25.197 1.00 98.02 C N
ATOM 7044N LEUC 299-38-741-15.364871 1.00 97.52 G C

ATOM 7045CA LEUC 299-38.680-15.9 . 1.00 98.36 C C
ATOM 7046CB LEUC 299-40.084-16.23923.329 1,00 99.06 C C
ATOM 7047CG LEUC 299-40.111-16.74421.879 1.00 99.16 C C
ATOM 7048CD1LEUC 299-39.336-18-05421.773 1.00 99.47 'CC
938 21.420 ATOM 7049CD2LEUC 299-41.548. 22,925 1.00 96.66 C C
ATOM 7050C LEUC 299-37.952- 22.717 1.00 96.69 C O
ATOM 7051O LEUC 299-38.380-15.023351 1,00 95.35 C N
-13.88522 ATOM 7052N LEUC 300-36.854. . 1.00 93.76 C C
ATOM 7053CA LEUC 300-36.054- 21.436 1.00 93.05 C C
ATOM 7054CB LEUC 300-34.634-14.70421.993 1.00 92.11 C C
-14.551419 ATOM 7055CG LEUC 300-34.536. . 1.00 91.81 C C
ATOM 7056CD1LEUC 300-33.075- 23.823 9.00 91.61 C C
ATOM 7057CD2LEUC 300-35.217-13.87123.496 1.00 93.09 C C
ATOM 7058C LEUC 300-36.015-12.62620.047 1.00 92.96 C O
ATOM 7059O LEUC 300-35.215-15.33519.777 1.00 92.35 C N
-16.230174 ATOM 7060N ASPC 301-36.891. . 1.00 91.92 C C
ATOM 7061CA ASPC 301-36.994-1 17.807 1.00 92.72 C C
ATOM 7062C8 ASPC 301-38.285-15.34917.171 1.00 93.40 C C
ATOM 7063CG ASPC 301-38.273-14.82415.656 1.00 93.63 C O
ATOM 7064OD1ASPC 301-38.147-14.92315.127 1.00 93.85 C O
-16.050996 ATOM 7065OD2ASPC 301-38.386. . 1.00 90.97 C C
ATOM 7066C ASPC 301-35.805- 16.914 1.00 91.24 C O
ATOM 7067O ASPC 301X4.896 -14.99216.722 1.00 89.46 C N
ATOM 7068N ASNC 302-35.823-15.80216.368 1.00 87.78 C C
-13.778471 ATOM 7469CA ASNC 302-34.771. . 1.00 87.60 C C
ATOM 7070CB ASN~ 302-35.289- 14.639 1.00 87.49 C C
ATOM 7071CG ASNC 302X5.832 -12.12715.498 1.00 87.48 C O
ATOM 7072OD1ASNC 302X5.112 -10.99716.318 1.00 86.82 C N
, -10.430313 ATOM 7073ND2ASN' 302-37.107-10.66. 1.00 86.88 C C
ATOM 7074C ASNC 302-33.469-12.90816.165 1.00 86.68 C O
ATOM 7075O ASN! 302-33.416-12.76217.390 1.00 85.27 C N

~ 12 15 C

ATOM 7076N TYRC 303-32.424. . 1.00 83.56 C C
ATOM 7077CA TYRC 30331.094 - 15.825 1.00 83.75 C C
ATOM 7078CB TYRC 30330.120 -12.35314.644 1.0D 84.09 C C
ATOM 7079CG TYRC 303-28.659-12.34315.010 1.00 84.37 C C
-12.182388 ATOM 7080CD1TYRC 303-27.887. . 9 1.0084:30 C C
ATOM 7081CE1TYRC 303-26.529- 15.68 6 1.0 0 84.28C C
ATOM 7082CD2TYRC 303 -28.038-13.1453 14.947 1.0 0 84.31C C
ATOM 7083CE2TYRC 303 -26.68-10.934 15.244 1.0 0 84.52 C
ATOM 7084CZ TYRC 303 -25.932 -10.784 15.614 1.0 0 84.5C C
5 -11.8989 3 O

ATOM 7085OH TYRC 303 -24.59. . 7 1.0 0 82.15 C
ATOM 7086C TYR C 3 -31.125 - 4 16.46 C
30 5 -10.96 ATOM7087O TYRC 303- -30.574_-10.753_17_5471.00 81.67 C 0 ATOM7088N SERC 304-31.776-10.022- 15.7901.00 80.38 C N

ATOM7089CA SERC 304-31.884-8.65 0 16.2721.00 78.83 C C

ATOM7090CB SERC 304-32.8$3-7.87415.408 1.00 78.94 C C

ATOM7091OG SERC 304-32.921-6.50515.772 1.00 79.10 C O

ATOM7092C SERC 304-32.297-8.56817.742 1.00 77.69 C C

ATOM7093O SERC 304-31.833-7.69118.473 1.00 77.51 C O

ATOM7094N ASPC 305-33.169-9.47818.171 1.00 76.39 C N

ATOM7095CA ASPC 305-33.629-9.50319.558 1.00 74.81 C C

ATOM7096CB ASPC 305-34.997-10.18819.673 1.00 76.65 C C

ATOM7097CG ASPC 305-36.114-9.39619.016 1.00 77.98 C C

ATOM7098OD1ASPC 305-36.253-8.18319.301 1.00 78.34 C O

ATOM7099OD2ASPC 305-36.867-10.00118.221 1.00 79.12 C O

ATOM7100C ASPC 305-32.645-10.23020.471 1.00 72.76 C C

ATOM71010 ASPC 305-32.391-9.79321.590 1.00 72.18 C O

ATOM7102N ARGC 306-32.103-11.34319.987 1.00 70.52 C N

ATOM7103CA ARGC 306-31.159-12.14920.753 1.00 68.75 C C

ATOM7104CB ARGC 306-30.825-13.42519.976 1.00 70.03 C C

ATOM7105CG ARGC 306-32.038-14.19419.453 1.0D 71.16 C C

ATOM7106CD ARGC 306-31.617-15.25018.431 1.00 72.28 C C

ATOM7107NE ARGC 306-31.576-16.61218.966 1.00 73.79 C N

ATOM7108CZ ARGC 306-30.980-16.96720.101 1.00 74.73 C C

ATOM7109NH1ARGC 306-30.365-16.06120.849 1.00 75.64 C N

ATOM7110NH2ARGC 306-30.985-18.23820.4$5 1.00 74.43 C N

ATOM7111C ARGC 306-29.862-11.38921.060 1.00 67.15 C C

ATOM7112O ARGC 306-29.283-11.52722.147 1.00 66.21 C O

ATOM7113N ILEC 307-29.408-10.59720.090 1.00 64.68 C N

ATOM7114CA ILEC 307-2$.183-9.81720.237 1.00 61.78 C C

ATOM7115CB ILEC 307-27.625-9.38418.847 1.00 61.08 C C

ATOM7116CG2ILEC 307-2$.431-8.21118.290 1.00 60.83 C C

ATOM7117CG1ILEC 307-26.148-9.01018.971 1.00 59.27 C C

ATOM71.18CD1ILEC 307-25.239-10.19819.240 1.00 57.96 C C

ATOM7119C ILEC 307-28.440-8.57821.097 1.00 60.27 C C

ATOM7120O ILEC 307-27.608-8.19921.922 1.00 58.98 C O

ATOM7121N GLNC 308-29.601-7.96120.908 1.00 58.98 C N

ATOM7122CA GLNC 308-29.965-6.77221.668 1.00 58.76 C C

ATOM7123CB GLNC 308-31.339-6.26821.218 1.00 60.03 C C

ATOM7124CG GLNC 308-31.849-5.04721.977 1.00 62.74 C C

ATOM7125CD GLNC 308-33.008-4.37021.264 1.00 64.21 C C

ATOM7126OE1GLNC 308-32.866-3.91820.125 1.00 65.58 C O

ATOM7127NE2GLNC 308-34.162-4.29821.927 1.00 64.46 C N

ATOM7128C GLNC 308-29.961-7.03223.178 1.00 57.59 C C

ATOM7129O GLNC 308-29.727-6.11523.969 1.00 57.71 C O

ATOM7130N VALC 309-30.221-8.27723.574 1.00 55.16 C N

ATOM7131CA VALC 309-30.220-8.63824.989 1.00 52.96 C C

ATOM7132CB VALC 309-31.030-9.94025.262 1.00 53-..40C C

ATOM7133CG1VALC 309-30.753-10.44426.673 1.00 52.10 C C

ATOM7134CG2VALC 309-32.518-9.67325.105 1.00 52.70 C C

ATOM7135C VALC 309-28.782-8.85625.427 1.00 50.98 C C
ATOM7136O VALC 309-28.389-8.46626.530 1.00 50.29 C O

ATOM7137N LEUC 310-27.997-9.48324.556 1.00 49.54 C N

ATOM7138CA LEUC 310-26.595-9.72824.861 1.00 49.13 C C

ATOM7139CB LEUC 310-25.957-10.61523.791 1.00 47.87 C C

ATOM7140CG LEUC 310-26.541-12.02223.697 1.00 47.54 C C
ATOM7141CD1LEUC 310-25.745-12.84722.708 1.00 47.38 C C

ATOM7142CD2LEUC 310-26.508-12.67025.067 1.00 48.29 C C

ATOM7143C LEUC 310-25.826-8.40924.977 1.00 48.82 C C

ATOM7144O LEUC 310-24.921-8.29025.806 1.00 49.60 C O

ATOM7145N GLNC 311-26.196-7.42224.159 1.00 47.13 C N

ATOM7146CA GLNC 311-25.535-6.11724.190 1.00 46,88 C C

ATOM7147CB GLNC 311-25.961-5.26322.986 1.00 46.70 C C

ATOM7148CG GLNC 311-25.569-5.85521.635 1.00 46.11 C C

ATOM7149CD GLNC 311-26.055-5.02520.457 1.00 45.57 C C

ATOM7150OE1GLNC 311-27.240-4.71320.351 1.00 46.12 C O
ATOM7151NE2GLNC 311-25.138-4.67319.561 1.00 44.50 C N

ATOM7152C GLNC 311-25.843-5.37125.486 1.00 46.23 C C

ATOM7153O GLNC 311-24.943-4.82126.117 1.00 45.52 C O

ATOM7154N ASNC 312-27.116-5.35025.875 1.00 45.58 C N

ATOM7155CA ASNC 312-27.519-4.68627.109 1.00 45.41 C C

ATOM7156CB ASNC 312-29.044-4.56927.176 1.00 45,21 C C

ATOM7157CG ASNC 312-29.593-3.54426.194 1.00 45.30 C C

ATOM7158OD1ASNC 312-29.504-2.33726.423 1.00 43.49 C O

ATOM7159ND2ASNC 312-30.153-4.02225.090 1.00 44,17 C N

ATOM7160C ASNC 312-26.998-5.48728.300 1.00 45.31 C C

ATOM7161O ASNC 312-26.659x.920 29.340 1.00 43.86 C O

ATOM7162N METC 313-26.925-6.80628.141 1.00 45.51 C N

ATOM7163CA METC 313-26.425-7.65329.218 1.00 46.43 C C

ATOM7164CB METC 313-26.468-9.13628.825 1.00 46.96 C C

ATOM7165CG METC 313-26.117-10.07829.977 1.00 49.11 C C

ATOM7166SD METC 313-26.093-11.84229.540 1.00 51.29 C S

ATOM7167CE METC 313-27.834-12.09629.160 1.00 51.56 C C

ATOM7168C METC 313-24.989-7.24729.533 1.00 45.40 C C

ATOM7169O METC 313-24.682-6.84330.658 1.00 45.73 C O

ATOM7170N VALC 314-24.115-7.34428.533 1.00 44.77 C N

ATOM7171CA VALC 314-22.707-6.98328.706 1.00 43.50 C C

ATOM7172CB VALC 314-21.897-7.32427.456 1.00 42.43 C C

ATOM7173CG1VAL 314-20.455-6.889- 27.6391.00 42.58C C
C

ATOM7174CG2VAL 314-21.966-8.81227.202 1.00 42.63C C
C

ATOM7175C VAL 314-22.550-5.49629.021 1.00 41.90C C
C

ATOM7176O VAL 314-21.614-5.08729.708 1.00 41.66C 0 C

ATOM7177N HIS 315-23.473-4.69228.513 1.00 41.01C N
C

ATOM7178CA HIS 315-23.447-3.26528.774 1.00 41.04C C
C

ATOM7179CB HIS 315-24.475-2.55027.887 1.00 39.10C C
C

ATOM7180CG HIS 315-24.540-1.06928.103 1,00 40.95C C
C

ATOM7181CD2HIS 315-25.597-0.24328.296 1.00 39.97C C
C

ATOM7182ND1HIS 315-23.417-0.27028.156 1.00 40.07C N
C

ATOM7183CE1HIS 315-23.7790.980 28.378 1.00 39.86C C
C

ATOM7184NE2HIS 315-25.0971.024 28.466 1.00 40.15C N
C

ATOM7185C HIS 315-23.766-3.08730.264 1.00 41.99C C
C

ATOM7186O HIS 315-23.146-2.25830.944 1.00 42.39C O
C

ATOM7187N CYS 316-24.720-3.88330.764 1.00 41.31C N
C

ATOM7188CA CYS 316-25.117-3.84332.175 1.00 40.80C C
C

ATOM7189CB CYS 316-26.313-4.76732.439 1.00 42.38C C
C

ATOM7190SG CYS 316-27.919-4.01432.141 1.00 43.82C S
C

ATOM7191C CYS 316-23.970-4.27233.058 1.00 39.14C C
C

ATOM7192O CYS 316-23.721-3.67334.099 1.00 38.88C O
C

ATOM7193N ALA 317-23.281-5.33132.649 1.00 38.42C N
C

ATOM7194CA ALA 317-22.137-5.81433.404 1.00 38.34C C
C

ATOM7195CB ALA 317-21.555-7.05332.734 1.00 37.56C C
C

ATOM7196C ALA 317-21.070-4.71033.495 1.00 39.96C C
C

ATOM7197O ALA 317-20.528-4.44034.574 1.00 39.83C O
C

ATOM7198N ASP 318-20.780-4.07132.360 1.00 39.87C N
C

ATOM7199CA ASP 318-19.772-3.01632.307 1.00 40.58C C
C

ATOM7200CB ASP 318-19.614-2.54530.853 1.00 41.82C C
C

ATOM7201CG ASP 318-18.419-1.62830.650 1.00 41.25C C
C

ATOM7202OD2ASP 318-18.621-0.57030.025 1.00 42.00C 0 C

ATOM7203C ASP 318-20.128-1.85233.240 1_.0_040.18C C
C

ATOM7204O ASP 318-19.256-1.24333.546 1.00 38.98C 0 ATOM7205OD1C 318-17.286-1.95231.091 1.00 43.71C O
ASP
C

ATOM7206N LEU 319-21.415-1.55433.362 1.00 41.49C N
C

ATOM7207CA LEU 319-21.861-0.48234.242 1.00 42.61C C
C

ATOM7208CB LEU 319-22.8670.413 33.508 1.00 42.61C C
C

ATOM7209CG LEU 319-22.4740.972 32.138 1.00 43.22C C
C

ATOM7210CDtLEU 319-23.5541.914 31.636 1.00 42.53C C
C

ATOM7211CD2LEU 319-21.1511.709 32.247 1.00 43.87C C
C

ATOM7212C LEU 319-2_2.520-1_.10535.486 1.00 43.82C C
i C

ATOM7213O LEU 319-23.565-0.64235.953 1.00 43.D9C O
C

ATOM7214N SER 320-21.901-2.14936.028 1.00 44.19C N
C

ATOM7215CA SER 320-22.466-2.82437.189 1.00 45.50C C
C

ATOM7216CB SER 320-22.400-4.33736.996 1.00 44.69C C
ATOM7217OG C 320-21.071-4.79937.154 1.00 43.59C O
SERC

ATOM7218C SER 320-21.833-2.48338.533 1.00 46.46C C
C

ATOM7219O SER 320-22.382-2.84539.570 1.00 47.51C O
ATOM7220N C 321-20.696-1.79538.544 1.00 46.48C N
ASN
C

ATOM7221CA ASN 321-20.075-1.49439.824 1.00 47.12C C
ATOM7222CB C 321-18.740-0.74939.642 1.00 47.51C C
ASN
C

ATOM7223CG ASN 321-18.8710.549 38.876 1.00 48.43C C
C

ATOM7224OD1ASN 321-19.2031.589 39.449 1.00 50.19C O
ATOM7225ND2C 321-18.6040.500 37.574 1.00 47.34C N
ASN
C

ATOM7226C ASN 321-20.989-0.76640.816 1.00 47.89C C
C

ATOM7227O ASN 321-20.900-0.99742.025 1.00 47.37C O
C

ATOM7228N PRO 322-21.8920.105 40.330 1.00 47.76C N
ATOM7229CD C 322-22.0020.708 38.989 1.00 47.83C C
PRO
C

ATOM7230CA PRO 322-22.7690.802 41.281 1.00 47.56C C
C

ATOM7231CB PRO 322-23.4371.878 40.422 1.00 47.42C C
ATOM7232CG C 322-22.4412.111 39.320 1.00 48.22C C
PRO
C

ATOM7233C PRO 322-23.806-0.11841.960 1.00 46.76C C
C

ATOM7234O PRO 322-24.3420.224 43.011 1.00 46.39C O
C

ATOM7235N THR 323-24.081-1.27341.357 1.00 46.18C N
C

ATOM7236CA THR 323-25.059-2.21541.904 1.00 45.30C C
C

ATOM7237CB THR 323-25.900-2.89640.787 1.00 44.64C C
C

ATOM7238OG1THR 323-25.114-3.90240.133 1.00 40.89C O
C

ATOM7239CG2THR 323-26.366-1.87039.756 1.00 43.54C C
C

ATOM7240C THR 323-24.405-3.32542.733 1.00 46.61C C
C

ATOM7241O THR 323-25.084-4.24343.189 1.00 46.39C O
C

ATOM7242N LYS 324-23.093-3.24442.928 1.00 46.71C N
C

ATOM7243CA LYS 324-22.384-4.25443.715 1.00 47.30C C
C

ATOM7244CB LYS 324-2D.957-4.45343.166 1.00 45.47C C
C

ATOM7245CG LYS 324-20.857-5.12141.802 1.00 44.86C C
C

ATOM7246CD LYS 324-21.542-6.48041.792 1.00 45.05C C
C

ATOM7247CE LYS 324-20.775-7.50340.971 1,00 46.D3C C
C

ATOM7248NZ LYS 324-20.400-7.02139.612 1.00 45.37C N
C

ATOM7249C LYS 324-22.300-3.84945.197 1.00 47.89C C
C

ATOM7250O LYS 324-22.551-2.69745.548 1.00 48.75C O
C

ATOM7251N PRO 325-21.955-4.80146.087 1.00 48.20C N
C

ATOM7252CD PRO 325-21.682-6.23145.836 1.00 47.78C C
C

ATOM7253CA PRO 325-21.839-4.49347.519 1.00 48.11C C
C

ATOM7254_CB PRO 325-21.213-5.76448.089 1.00 48.02C C
C

ATOM7255CG PRO 325-21.792-6.83447.214 1.00 48.06C C
C

ATOM7256C PRO 325-20.930-3.27247.706 1.00 48.68C C
C

ATOM7257O PRO 325-19.807-3.24647.200 1.00 48.37C O
C

ATOM7258N LEU 326-21.416-2.27348.437 1.00 49.07C N
C

ATOM 7259CA LEUC 326-20.674-1.03348.6731.00 49.09 C C

ATOM 7260CB LEUC 326-21.175-0.36249.9481.00 48.78 C C

ATOM 7261CG LEUC 326-20.7121.081 50.1241.00 47.54 C C

ATOM 7282CD1LEUC 326-21.1731.904.48.9251.00 46.77 C C

ATOM 7263CD2LEUC 326-21.2791.640 51.4121.00 48.14 C C

ATOM 7264C LEUC 326-19.156-1.18548.7551.00 49.32 C C

ATOM 7265O LEUC 326-18.406-0.40348.1711.00 48.95 C O

ATOM 7266N GLNC 327-18.710-2.17949.5051.00 50.32 C N

ATOM 7267CA GLNC 327-17.286_ _ 1.00 51.34 C C
-2.45349.663 ATOM 7268CB GLNC 327-17.146-3.77650.4081.00 52.97 C C

ATOM 7269CG GLNC 327-15.820x.459 50.2971.00 55.67 C C

ATOM 7270CD GLNC 327-15.944-5.91150.6941.00 58.40 C C

ATOM 7271OE1GLNC 327-16.700-6.66850.0721.00 59.64 C O

ATOM 7272NE2GLNC 327-15.220-6.31259.7401.00 58.75 C N

ATOM 7273C GLNC 327-16.577-2.50948.2931.00 50.74 C C

ATOM 7274O GLNC 327-15.470-1.99048.1241.00 49.71 C O

ATOM 7275N LEUC 328-17.227-3.14447.3221.00 49.64 C N

ATOM 7276CA LEUC 328-16.682-3.25245.9751.00 49.74 C C

ATOM 7277CB LEUC 328-17.398-4.36245.2051.00 49.41 C C

ATOM 7278CG LEUC 328-17.186-5.80345.6711.00 50.11 C C

ATOM 7279CD1LEUC 328-18.248-6.69045.0391.00 49.24 C C

ATOM 7280CD2LEUC 328-15.772-6.27245.3031.00 49.70 C C

ATOM 7281C LEUC 328-16.860-1.92745.2291.00 49.63 C C

ATOM 7282O LEUC 328-15.893-1.34144.7391.00 50.50 C O

ATOM 7283N TYRC 329-18.106-1.47045.1451.00 48.51 C N
ATOM 7284CA TYRC 329-18.444-0.22644.4631.00 48.17 C C

ATOM 7285CB TYRC 329-19.9010.157 44.7821.00 48.18 C C

ATOM 7286CG TYRC 329-20.4011.457 44.1701.00 48.10 C C

ATOM 7287CD1TYRC 329-19.9061.929 42,9531.00 47.73 C C

ATOM 7288CE1TYRC 329-20.3983.112 42.3811.00 48.01 C C

ATOM 7289CD2TYRC 329-21.4032.200 44.8001.00 48.70 C C

ATOM 7290CE2TYRC 329-21.9023.375 44.2381.00 47.69 C C

ATOM 7291CZ TYRC 329-21.3983.826 43.0321.00 47.91 C C

ATOM 7292OH TYRC 329-21.9034.981 42.4821.00 47.73 C O

ATOM 7293C TYRC 329-17.4960.892.44.8631.00 48.03 C C

ATOM 7294O TYRC 329-17.0611.675 44.0211.00 47.53 C O

ATOM 7295N ARGC 330-17.1660.954 46.1471.00 48.03 C N

ATOM 7296CA ARGC 330-16.2741.958 46.6441.00 48.37 C C

ATOM 7297CB ARGC 330-16.1811.919 48.1701.00 50.47 C C

ATOM 7298CG ARGC 330-17.2002.796 48.8731.00 53.89 C C

ATOM 7299CD ARGC 330-16.5264.023 49.4701.00 56.51 C C

ATOM 7300NE ARGC 330-16.0383.757 50.8201.00 58.58 C N

ATOM 7301CZ ARGC 330-15.0064.375 51.3841.00 58.89 C C

ATOM 7302NH1ARGC 330-14.3305.304 50.7161.00 59.02 C N

ATOM 7303NH2ARGC 330-14.6544.066 52.6221,00 59.91 C N

ATOM 7304C ARGC 330-14.8861.908 46.0301,00 47.66 C C

ATOM 7305O ARGC 330-14.2782.936 45.7301.00 47.14 C O

ATOM 7306N GLNC 331-14.3730.697 45.8461.00 46.60 C N

ATOM 7307CA GLNC 331-13.0540.561 45.2521.00 46.77 C C

ATOM 7308CB GLNC 331-12.541-0.86945.4021.00 46.64 C C

ATOM 7309CG GLNC 331-12.215-1.19146.8481,00 49.14 C C

ATOM 7310CD GLNC 331-11.693-2.59447.0441.00 50.59 C C

ATOM 7311OE1GLNC 331-10.534-2.89246.7391.00 50.78 C O

ATOM 7312NE2GLNC 331-12.554-3.47447.5501.00 51.16 C N

ATOM 7313C GLNC 331-13.0980.978 43.7911.00 46.22 C C

ATOM 7314O GLNC 331-12.1831.638 43.3011,00 46.73 C O

ATOM 7315N TRPC 332-14.1720.618 43.1011.00 44.58 C N

ATOM 7316CA TRPC 332-14.3100.987 41.7031.00 45.04 C C
ATOM 7317CB TRPC 332-15.5660.343 41.1081.00 44.37 C C

ATOM 7318CG TRPC 332-15.424-1.13640.8641,00 44 C C

ATOM 7319CD2TRPC 332-14.380-1.79140.1301.00 . C C
44.69 ATOM 7320CE2TRPC 332-14.657-3.17940.1561.00 43.91 C C
ATOM 7321CE3TRPC 332-13.236-1.34139.4521.00 43 C C

ATOM 7322CD1TRPC 332-16.269-2.12741.2911.00 . C C

ATOM 7323NE7TRPC 332-15.814-3.35340.8681.00 . C N

18 ATOM 7324CZ2TRPC 332-13.829-4.12339.5301.00 . C C
ATOM 7325CZ3TRPC 332-12.415-2.28038.8291.00 43.52 C C
ATOM 7326CH2TRPC 332-12.718-3.65638.8741.00 43.17 C C
ATOM 7327C TRPC 332-14.3702.510 41.5491.00 41.90 C C
ATOM 7328O TRPC 332-13.6933.089 40.7051.00 45.01 C O
ATOM 7329N THRC 333-15.1713.159 42.3791.00 44.80 C N
ATOM 7330CA THRC 333-15.3064.601 42.3171.00 45.02 C C
44.28 ATOM 7331CB THRC 333-16.3615.076 43.3261.00 44.43 C C
ATOM 7332OG1THRC 333-17.6334.539 42.9421 45 C O

ATOM 7333CG2THRC 333-16.4576.592 43.356. . C C
ATOM 7334C THRC 333-13.9745.308 42.5431,00 44.24 C C
ATOM 7335O THRC 333-13.5946.187 41.7651.00 44.32 C O
ATOM 7336N ASPC 334-13.2474.931 43.5861.00 44.59 C N
ATOM 7337CA ASPC 334-11.9645.577 43.8241.00 44.28 C C

ATOM 7338CB ASPC 334-11.3385.092 45.138. . C C
1;00 47 ATOM 7339CG ASPC 334-12.1475.516 46.3701.00 . C C
ATOM 7340OD1ASPC 334-12.7056.639 46.3761.00 49.93 C O
ATOM 7341OD2ASPC 334-12.2134.731 47.3421.00 51.29 C O
ATOM 7342C ASPC 334-11.0125.326 42.6461.00 51.27 C C
ATOM 7343O ASPC 334-10.2086.190 42.2951.00 43.74 C O
ATOM 7344N ARGC 335-11.1174.153 42.0301.00 43.91 C N
42.39 ATOM7345CA ARGC 335-10.2763.810 40.8891.00 41.40 C C

ATOM7346CB ARGC 335-10.3432.304 40.6161.00 41.72 C C

ATOM7347CG ARGC 335-9.479 1.434 41.5451.00 41.39 C C

ATOM7348CD ARGC 335-9.789 -0.04341.3221.00 42.03 C C

ATOM7349NE ARGC 335-8.898 -0.93342.0511.00 43.05 C N

ATOM7350CZ ARGC 335-7.613 -1.11541.7641.00 44.08 C C

ATOM7351NH1ARGC 335-7.057 -0.46840.7491.00 43.71 C N

ATOM7352NH2ARGC 335-6.879 -1.94042.5031.00 43.27 C N

ATOM7353C ARGC 335-10.6704.591 39.6291.00 41.19 C C

ATOM7354O ARGC 335-9.804 5.123 38.9421.00 41.60 C O

ATOM7355N ILEC 336-11.9664.674 39.3301.00 41.16 C N

ATOM7356CA ILEC 336-12.4335.406 38.1461.00 41.75 C C

ATOM7357CB ILEC 336-13.9805.290 37.9621.00 41.79 C C

ATOM7358CG2ILEC 336-14.7036.188 38.9521.0D 41.57 C C

ATOM7359CG1ILEC 336-14.3885.733 36.5541.00 42.59 C C

ATOM7360CDtILEC 336-14.1934.684 35.4891.00 42.34 C C

ATOM7361C ILEC 336-12.0676.887 38.2721.00 42.00 C C

ATOM7362O ILEC 336-11.5837.504 37.3251.0D 40.60 C O

ATOM7363N METC 337-12.2977.446 39.4561.00 42.81 C N

ATOM7364CA METC 337-12.0018.847 39.7131.00 43.52 C C

ATOM7365CB METC 337-12.4599.252 41.1181.00 43.89 C C

ATOM7366CG METC 337-13.9719.300 41.2821.00 45.51 C C

ATOM7367SD METC 337-14.77710.29740.0081.00 47.44 C S

ATOM7368CE METC 337-14.30911.95140.5161.00 47.33 C C

ATOM7369C METC 337-10.5239.132 39.5671.00 43.20 C C

ATOM7370O METC 337-10.13810.17139.0421.00 42.42 C O

ATOM7371N GLUC 338-9.693 8.214 40.0421.00 43.76 C N

ATOM7372CA GLUC 338-8.256 8.403 39.9361.00 44.53 C C

ATOM7373CB GLUC 338-7.521 7.212 40.5401.00 45.03 C C

ATOM7374CG GLUC 338-6.021 7.421 40.6691.00 47.69 C C
ATOM7375CD GLUC 338-5.313 6.193 41.2261.00 49.33 C C

ATOM7376OE1GLUC 338-5.901 5.505 42.0991.00 50.06 C O

ATOM7377OE2GLUC 338-4.170 5.926 40.7981.00 49.51 C 0 ATOM7378C GLUC 338-7.885 8.543 38.4621.00 43.65 C C

ATOM7379O GLUC 338-7.039 9.352 38.0911.00 44.10 C O

ATOM7380N GLUC 339-8.541 7.756 37.6211.00 42.74 C N

ATOM7381CA GLUC 339-8.265 7.786 36.1941.00 42.72 C C

ATOM7382CB GLUC 339-8.891 6.562 35.5291.00 43.40 C C

ATOM7383CG GLUC 339-8.209 6.138 34.2561.00 43.51 C C

ATOM7384CD GLUC 339-8.749 4.830 33.7231.00 44.35 C C

ATOM7385OE1GLUC 339-8.593 3.786 34.4041.00 44.44 C O

ATOM7386OE2GLUC 339-9.335 4.853 32.6231.00 43.95 C O

ATOM7387C GLUC 339-8.778 9.077 35.5531.00 41.70 C C

ATOM7388O GLUC 339-8.122 9.651 34.6921.00 40.28 C O

ATOM7389N PHEC 340-9.946 9.542 35.9751.00 40.99 C N
ATOM7390CA PHEC 340-10.47710.77935.4221.00 41.41 C C

ATOM7391CB PHEC 340-11.89711.04135.9281.00 42.68 C C

ATOM7392CG PHEC 340-12.93610.11935.3551.00 44.70 C C

ATOM7393CD1PHEC 340-12.6739.357 34.2261.00 46.49 C C

ATOM7394CD2PHEC 340-14.20310.05235.9231.00 45.86 C C

ATOM7395CE1PHEC 340-13.6628.542 33.6701.00 48.04 C C

ATOM7396CE2PHEC 340-15.1919.245 35.3741.00 46.75 C C

ATOM7397CZ PHEC 340-14.9228.491 34.2471.00 47.00 C C
ATOM7398C PHEC 340-9.589 11.96335.8091.00 40.75 C C

ATOM7399O PHEC 340-9.313 12.84234.9891.00 39.96 C O

ATOM7400N PHEC 341-9.147 11.98237.0611.00 40.34 C N

ATOM7401CA PHEC 341-8.302 13.06737.5451.00 41.43 C C
ATOM7402CB PHEC 341-8.042 12.95439.0591.00 42.26 C C
ATOM7403CG PHEC 341-9.264 13.17439.9171.00 43.62 C C

ATOM7404CD1PHEC 341-10.37813.84939.4201.00 44.89 C C

ATOM7405CD2PHEC 341-9.283 12.73441.2371.00 44.72 C C

ATOM7406CE1PHEC 341-11.49214.08240.2261.00 46.31 C C
ATOM7407CE2PHEC 341-10.39012.96142.0531.00 45.81 C C

ATOM7408CZ PHEC 341-11.49_813.63641.5461.00 46.45 C C

ATOM7409C PHEC 341-6..97613.05736.8151.00 41.32 C C

ATOM7410O PHEC 341-6.430 14.10936.5021.00 39.96 C O

ATOM7411N ARGC 342-6.451 11.86536.5551.00 42.07 C N

ATOM7412CA ARGC 342-5.184 11.77235.5621.00 43.02 C C

ATOM7413CB ARGC 342-4.632 10.34835.9111.00 46.18 C C

ATOM7414CG ARGC 342-3.220 10.25135.3761.00 52.19 C C

ATOM7415CD ARGC 342-2.578 8.913 35.7191.00 58.45 C C

ATOM7416NE ARGC 342-1.290 8.739 35.0411.00 62.77 C N

ATOM7417CZ ARGC 342-0.549 7.634 35.1101.00 65.28 C C

ATOM7418NH1ARGC 342-0.964 6.596 35.8341.00 65.65 C N

ATOM7419NH2ARGC 3420.603 7.560 34.4441.00 65.24 C N

ATOM7420C ARGC 342-5.377 12.25534.4241.00 41.65 C C

ATOM7421O ARGC 342-4.515 12.95833.8921.00 39.91 C O

ATOM7422N GLNC 343-6.501 11.90733.7981.00 39.87 C N

ATOM7423CA GLNC 343-6.747 12.40132.4431.00 40.11 C C

ATOM7424CB GLNC 343-8.058 11.86531.8441.00 39.84 C C

ATOM7425CG GLNC 343-8.426 12.59930.5411.00 40.60 C C

ATOM7426CD GLNC 343-9.491 11.90729.7061.00 41.98 C C

ATOM7427OE1GLNC 343-9.503 10.68429.5801.00 43.51 C 0 ATOM7428NE2GLNC 343-10.37412.69629.1001.00 41.41 C N

ATOM7429C GLNC 343-6.834 13.92732.5231.00 40.27 C C

ATOM7430O GLNC 343-6.334 14.64031.6491.00 39.72 C O

ATOM 7431N GLYC 344-7.47614.416 33.5821.00 40.14 C N

ATOM 7432CA GLYC 344-7.61115.846 3_3.776_ 40.45 C ' 1.00 C

ATOM 7433C GLYC 344-6.26916.537 33.8961.00 41.28 C C

ATOM 74340 GLYC 344-6.08217.616 33.3371.00 41.91 C O

ATOM 7435N ASPC 345-5.33715.932 34.6331.00 42.36 C N

ATOM 7436CA ASPC 345-3.99516.500 34.7921.00 42.65 C C

ATOM 7437CB ASPC 345-3.12415.617 35.6891.00 42.78 C C

ATOM 7438CG ASPC 345-3.55515.649 37.1311.00 45.25 C C

ATOM 7439OD1ASPC 345-4.33816.556 37.4811.00 46.91 C O

ATOM 7440OD2ASPC 345-3.10314.785 37.9191.00 45.77 C O

ATOM 7441C ASPC 345-3.34916.576 33.4171.00 43.32 C C

ATOM 74420 ASPC 345-2.75217.558 33.0411.00 43.31 C O

ATOM 7443N ARGC 346-3.47015.479 32.6771.00 43.47 C N

ATOM 7444CA ARGC 346-2.92015.385 31.3371.00 4 C C
4.71 ATOM 7445CB ARGC 346-3.26014.02D 30.7291.00 _ C C
44.34 ATOM 7446CG ARGC 346-2.58112.867 31.4341.00 44.28 C C

ATOM 7447CD ARGC 346-1.71012.111 30.4771.00 45.7 C C

ATOM 7448NE ARGC 346-2.37010.901 3p.0141.00 _ C N
48.4 ATOM 7449CZ ARGC 346-2.09110.277 28.8731.00 _ C C
48.83 ATOM 7450NH1ARGC 346-1.15610.747 28.0521.00 48.61 C N

ATOM 7451NH2ARGC 346-2.7449.167 28.5601.00 50.51 C N

ATOM 7452C ARGC 346-3.45916.511 30.4581.00 45.25 C C

ATOM 7453O ARGC 346-2.70217.152 29.7351.00 44.80 C O

ATOM 7454N GLUC 347-4.76516.757 30.5291.00 45.66 C N

ATOM 7455CA GLUC _34_7-5.36517.817 29.7321.00 46.61 C C

ATOM 7456CB GLUC 347-6.89417.725 29.7901.00 46.55 C C

ATOM 7457CG GLUC 347-7.44316.402 29.2841.00 _ C C
45.39 ATOM 7458CD GLUC 347_-8.94416.278 29.4461.00 44.71 C C

ATOM 7459OE1GLUC 347-9.46616.697 30.4961.00 44.68 C O

ATOM 7460OE2GLUC 347-9.60415.738 28.5341.0 44.85 C O

ATOM 7461C GLUC 347-4.89719.181 30.237_ 48.09 C C
1.00 ATOM 7462O GLUC 347-4.69620.105 29.4541.00 47.82 C O

ATOM 7463N ARGC 348-4.71319.300 31.5491.00 49.90 C N

ATOM 7464CA ARGC 348-4.2602D.556 32.1351.00 51.74 C C

ATOM 7465CB ARGC 348-4.48520.557 33.6521.00 _ C C
53.22 ATOM 7466CG ARGC 348-4.15921.893 34.3111.00 72 C C
54.

ATOM 7467CD ARGC 348-4.13521.795 35.8241.D0 _ C C
57.12 ATOM 7468NE ARGC 348-5.39621.292 36.3621.00 59.79 C N

ATOM 7469CZ ARGC 348-5.53720.112 36.9661.00 60.53 C C

ATOM 7470NHtARGC 348-4.49019.305 37.1131.00 58.30 C N

ATOM 7471NH2ARGC 348-6.73119.738 37.4171.00 60.18 C N

ATOM 7472C ARGC 348-2.77620.782 31.8341.00 52.65 C C

ATOM 7473O ARGC 348-2.25821.884 32.0161.00 52.07 C O

ATOM 7474N GLUC 349-2.09619.727 31.3851.00 53.62 C N

ATOM 7475CA GLUC 349_-0.67719.805 31.0321.00 54.23 C C

ATOM 7476CB GLUC 349-0.04718.410 30.9421.00 53.67 C C

ATOM 7477CG GLUC 349_0.16917.709 32.252__ 53.21 C C
1.00 ATOM 7478CD GLUC 3491.011 16.457 32.0991.00 52.91 C C

ATOM 7479OE1GLUC 3490.659 15.594 31.2651.00 50.55 C O

ATOM 7480OE2GLUC 3492.023 16.340 32.8261.00 53.46 C O

ATOM 7481C GLUC 349-0.50820.471 29.6721.00 54.59 C C

ATOM 7482O GLUC 3490.433 21.235 29.4511.00 53.83 C O

ATOM 7483N ARGC 350-1.42020.145 28.7591.00 55.0D C N

ATOM 7484CA ARGC 350-1.39020.674 27.4041.00 55.56 C C

ATOM 7485CB ARGC 350_-1.79019.578 26.4141.D0 55.58 C C

ATOM 7486CG ARGC 350-0.98818.290 26.5351.00 53.69 C C

ATOM 7487CD ARGC 350-1.92117.115 26.7731.00 51.74 C C

ATOM 7488NE ARGC 350-1.24415.820 26.754_ 48,85 C N
1.00 ATOM 7489CZ ARGC 350-0.79715.222 25.6561.00 47.19 C C

ATOM 7490NH1ARGC 350-0.94815.803 24.4781.00 46.83 C N

ATOM 7491NH2ARGC 350-0.2_2014.032 25.7351.00 46.82 C N

ATOM 7492C ARGC 350-2.32821.865 27,2491.00 56.15 C C

ATOM 7493O ARGC 350-2.50422.386 26.1 1.00 55.65 C O

ATOM 7494N GLYC 351-2.93922.280 _ 1.00 57.39 C N
28.353 ATOM 7495CA GLYC 351-3.85423.407 28.3121.00 59.33 C C

ATOM 7496C GLYC 351-5.18423.167 27.6111.00 60.63 C C

ATOM 7497O GLYC 351-5.74124.091 _ 1.00 61.72 C O
--27.022 ATOM 7498N METC 352-5.69921.942 _ 1.00 61.62 C N
27.664 ATOM 7499CA METC 352-6.98421.618 27.0381.00 62.72 C C

ATOM 7500CB METC 352-7.02920.137 26.6451.00 61.44 C C

ATOM 7501CG METC 352-5.99019.706 25.6241.00 60.52 C C

ATOM 7502SD METC 352-5.83217.901 25.5281.00 60.13 C S

ATOM 7503CE METC 352-6.92317.504 24.1641.00 59.49 C C

ATOM 7504C METC 352-8.07721.887 28.0671.00 64.34 C C

ATOM 7505O METC 352-7.77922.068 _ 1.00 64.88 C O
29.248 ATOM 7506N GLUC 353-9.33521.922 27.6331.00 65.85 C N

ATOM 7507CA GLUC 353-10.4302_2.13628.5781.00 67.32 C C

ATOM 7508CB GLUC 353-11.77722.319 27.8601.00 68.19 C C

ATOM 7509CG GLUC 353-11.83323.435 26.8231.00 70.58 C C

ATOM 7510CD GLUC 353-13.22023.580 26.1931.00 71.13 C C

ATOM 7511OE1GLUC 353-13.83422.546 25.8461.00 71.33 C O

ATOM 7512OE2GLUC 353-13.69324.728 26.0351.00 71.27 C O

ATOM 7513C GLUC 353-10.49220.862 29.4151.00 67.40 C C

ATOM 75140 GLUC 353-10.50319.759 28.8631.00 67.33 C O

ATOM 7515N ILEC 354-10.52121.004 30.7351,00 67.41 C N

I 7516CA ILEC 354-10.59119.833 31.6011.00 67.56 C C
ATOM

ATOM 7517CB ILEC 354-10.39520.22033.0861.00 67.00 C C

ATOM 7518CG2ILEC 354-10.51918.98633.9711.00 66.43 C C

ATOM 7519CG1ILEC 354-9.013 20.85033.2771.00 66.63 C C

ATOM 7520CD1ILEC 354-8.702 21.25134.7141.00 66.53 C C

ATOM 7521C ILEC 354-11.94519.14531.4211.00 67.92 C C

ATOM 7522O ILEC 354-12.99519.76031.5961.00 68.10 C O

ATOM 7523N SERC 355-11.91317.86931.0551.00 68.62 C N

ATOM 7524CA SERC 355-13.13417.09830.8391.00 69.45 C C

ATOM 7525CB SERC 355-12.77515.67030.4201.00 68.78 C C

ATOM 7526OG SERC 355-12.07415.66829.1901.00 68.21 C O

ATOM 7527C SERC 355-14.02517.06632.0861.00 70.63 C C

ATOM 7528O SERC 355-13.58617.43033.1821.00 70.68 C O

ATOM 7529N PROC 356-15.29716.64731.9321.00 71.40 C N

ATOM 7530CD PROC 356-16.00316.46230.6481.00 71.89 C C

ATOM 7531CA PROC 356-16.24716.57133.0501.00 71.66 C C

ATOM 7532CB PROC 356-17.57416.25032.3601.00 71.79 C C

ATOM 7533CG PROC 356-17.41516.86331.0051.00 71.71 C C

ATOM 7534C PROC 35fi-15.86115.49434.0651.00 71.90 C C

ATOM 7535O PROC 356-15.57214.35433.6901.00 72.00 C O

ATOM 7536N METC 357-15.86715.86135.3431.00 71.61 C N

ATOM 7537CA METC 357-15.51614.94236.4261.00 71.37 C C

ATOM 7538CB METC 357-16.23813.59636.2671.00 71.48 C C

ATOM 7539CG METC 357-17.75413.63836.3731.00 71.17 C C

ATOM 7540SD METC 357-18.48411.97336.3521.00 71.44 C S

ATOM 7541CE METC 357-18.81511.74834.5961.00 70.94 C C

ATOM 7542C METC 357-14.01314.67536.4921.00 71.04 C C

ATOM 7543O METC 357-13.54813.97937.3951.00 70.87 C O

ATOM 7544N CYSC 358-13.25615.22535.5441.00 70.50 C N

ATOM 7545CA CYSC 358-11.80815.01035.5041.00 70.59 C C

ATOM 7546CB CYSC 358-11.33614.88334.0501.00 69.73 C C

ATOM 7547SG CYSC 358-11.98313.43733.1761.00 69.19 C S

ATOM 7548C CYSC 358-10.94916.05836.2161.00 70.89 C C

ATOM 7549O CYSC 358-9.719 15.99236.1561.00 69.83 C O

ATOM 7550N ASPC 359-11.58217.01636.8901.00 71.57 C N

ATOM 7551CA ASPC 359-10.82618.05437.5911.00 72.77 C C

ATOM 7552CB ASPC 359-11.40619.43537.2891.00 74.19 C C

ATOM 7553CG ASPC 359-10.61120.54737.9401.00 75.51 C C

ATOM 7554OD1ASPC 359-9.367 20.54737.8091.00 75.97 C O

ATOM 7555OD2ASPC 359-11.22521.42538.5801.00 77.39 C O

ATOM 7556C ASPC 359-10.76917.84239.1021.00 72.72 C C

ATOM 7557O ASPC 359-11.75418.04939.8131.00 72.08 C O

ATOM 7558N LYSC 360-9.593 17.44739.5811.00 73.30 C N

ATOM 7559CA LYSC 360-9.371 17,17640.9971.00 73.90 C C

ATOM 7560CB LYSC 360-8.030 16.47341.1901.00 73.71 C C

ATOM 7561CG LYSC 360-6.823 17.33340.8481.00 73.16 C C

ATOM 7562CD LYSC 360-5.539 16.59941.1891.00 72.89 C C

ATOM 7563CE LYSC 360-4.313 17.40440.8041.00 72.53 C C

ATOM 7564NZ LYSC 360-3.064 16.66641.1181.00 71.50 C N

ATOM 7565C LYSC 360-9.414 18.39341.9151.00 74.54 C C

ATOM 7566O LYSC 360-9.340 18.24343.1321.00 74.32 C O

ATOM 7567N NISC 361-9.515 19.59141.3481.00 75.63 C N

ATOM 7568CA HISC 361-9.563 20.80242.1681.00 76.51 C C

ATOM 7569CB HISC 361-8.576 21.84641.6301.00 76.55 C C

ATOM 7570CG HISC 361-7.143 21.40441.6851.00 77.01 C C

ATOM 7571CD2HISC 361-6.147 21.48740.7711.00 77.35 C C

ATOM 7572ND1HISC 361-6.592 20.80042.7961.00 77.10 C N

ATOM 7573CE1HISC 3615.320 20.52842.5631.00 77.14 C C

ATOM 7574NE2HISC 3615.024 20.93541.3421.00 77.53 C N

ATOM 7575C HISC 361-10.98321.37042.2381.00 76.87 C C

ATOM 7576O HISC 361-11.27222.29143.0081.00 76.76 C 0 ATOM 7577N ASNC 362-11.86320.79541.4251.00 77.23 C N

ATOM 7575CA ASNC 362-13.26721.17741.3751.00 77 C C

ATOM 7579CB ASNC 362-13.52322.16940.2331.00 . C C
79.30 ATOM 7580CG ASNC 362-14.93822.73640.2521.00 80.37 C C

ATOM 7581OD1ASNC 362-15.92022.00340.1021.00 80.93 C O
ATOM 7582ND2ASNC 362-15.04624.04840.4421.00 81.03 C N

ATOM 7583C ASNC 362-14.03119.88141.1291.00 76.99 C C

ATOM 7584O ASNC 362-14.65719.69640.0841.00 76 C O

ATOM 7585N ALAC 363-13.95418.98042.1051.00 . C N

ATOM 7586CA ALAC 363-14.61017.68342.0141.00 . C C
ATOM 7587CB ALAC 3fi3-13.58716.57442.2331.00 75.01 C C
ATOM 7588C ALAC 363-15.75517.52643.0021.00 75.34 C C
ATOM 75890 ALAC 363-15.80518.19244.0391.00 74.17 C O
ATOM 7590N SERC 364-16.67316.63042.6601.00 74.04 C N
ATOM 7591CA SERC 364-17.83316.32343.4861.00 73.08 C C

ATOM 7592CB SERC 364-19.05517.08542.9741.00 . C C
ATOM 7593OG SERC 364-18.73618.44642.7291.00 72.64 C O
ATOM 7594C SERC 364-18.05914.81743.3511.00 73.90 C C
ATOM 7595O SERC 364-19.10914.37142.8811.00 70.13 C 0 ATOM 7596N VALC 365-17.05014.04643.7521.00 69.28 C N
ATOM 7597CA VALC 365-17.08912.59043.6741 68.31 C C

ATOM 7598CB VALC 365-15.97711.97144.546. . C C
ATOM 7599CG1VALC 365-15.95310.45944.3501.00 66.82 C C
ATOM 7600CG2VALC 365-14.63612.56344.1571.00 66.95 C C
ATOM 7601C VALC 365-18.44512.02844.0911.00 66.81 C C
1 7602O VALC 365-19.04211.23143.3661.00 65.80 C O
ATOM 1.00 65.50 ATOM7603N GLUC 366-18.93112.45245.254 1.00 65.19 C N

ATOM7604CA GLUC 366-20.22711.99945.754 1.00 64.42 C C

ATOM7605CB GLUC 366-20.53112.62147.119 1.00 64.56 C C

ATOM7606CG GLUC 366-19.49512.36248.196 1.00 65.54 C C

ATOM7607CD GLUC 366-18.18313.08447.944 1.00 65.93 C C

ATOM7608OE1GLUC 366-18.21514.18447.353 1.00 66.11 C O

ATOM7609OE2GLUC 366-17.12212.56248.351 9.00 65.74 C O

ATOM7610C GLUC 366-21.33412.39244,781 1.00 63.74 C C

ATOM7611O GLUC 366-22.09811.54044.323 1.00 63.13 C O

ATOM7612N LYSC 367-21.41113.6$644.472 1.00 63.75 C N

ATOM7613CA LYSC 367-22.42414.20943.557 1.00 63.88 C C

ATOM7614CB LYSC 367-22.21115.70543.321 1.00 64.45 C C

ATOM7615CG LYSC 367-22.30516,54544.576 1.00 66.47 C C

ATOM7616CD LYSC 367-22.21718.03144.252 1.00 67.75 C C

ATOM7617CE LYSC 367-22.30818.87945.510 1.00 68.32 C C

ATOM7618NZ LYSC 367-22.26720.33445.193 1.00 69.00 C N

ATOM7619C LYSC 367-22.41113.48642,218 1.00 63.26 C C

ATOM7620O LYSC 367-23.46313.10441.696 1.00 63.24 C O

ATOM7621N SERC 368-21.21613.30541.665 1.00 62.36 C N

ATOM7622CA SERC 368-21.06412.62840.386 1.00 62.04 C C

ATOM7623CB SERC 368-19.58612.56839.994 1.00 63.11 C C

ATOM7624OG SERC 368-19.09313.86139.887 1.00 64.41 C O
ATOM7625C SERC 368-21.64711.22040.425 1.00 61.08 C C

ATOM7626O SERC 368-22.40610.83439.536 1.00 60.90 C O

ATOM7627N GLNC 369-21.29410.45941.457 1.00 60.05 C N

ATOM7628CA GLNC 369-21.7959.096 41.597 1.00 58.30 C C

ATOM7629CB GLNC 369-21.2558.457 42.874 1.00 57.93 C C
' ATOM7630CG GLNC 369-19.7618.222 42.833 1.00 56.83 C C

ATOM7631CD GLNC 369-19.3367.473 41.584 1.00 56.86 C C
ATOM7632OE1GLNC 369-19.5326.381 41,302 1.00 55.66_C O

ATOM7633NE2GLNC 369-18.4148.060 40.824 1.00 56.52 C N

ATOM7634C GLNC 369-23.3119.066 41.602 1.00 57.49 C C
ATOM7635O GLNC 369-23.9198.293 40.861 1.00 57.05 C O
ATOM7636N VALC 370-23.9249.908 42.431 1.00 57.22 C N

ATOM7637CA VALC 370-25.3829.959 42.489 1.00 56.71 C C

ATOM7638CB VALC 370-25.88210.96343.551 1.00 57.42 C C

ATOM7639CG1VALC 370-27.39811.10843.457 1.00 57.51 C C
ATOM7640CG2VALC 370-25.49610.47944.947 1.00 57.51 C C

ATOM7641C VALC 370-25.91610.36541.122 1.00 55.37 C C

ATOM7642O VALC 370-26.9239.83 40.657 1.00 54.70 C O

ATOM7643N GLYC 371-25.222_ 40_.4761.00 55.27 C N
ATOM7644CA GLYC 371-25.63711.2969.157 1.00 54.33 C C
11.7443 ATOM7645C GLYC 371-25.550__10.620_ _1.00 53.95 C C
ATOM7646O GLYC 3 -2&.49210.39 3_8.144_1.00 54.16 C O
71 8 37.381 ATOM7647N PHEC _ -24.423_ 38.147 1.00 53.47 C N
372 9.906 ATOM7648CA PHEC 372-24.1868.793 37.229 1.00 52.85 C C
ATOM7649CB PHEC 372-22.7828.209 37.468 1.00 52.11 C C
ATOM7650CG PHEC 372-22.4277.046 36.567 1.00 50.77 C C

ATOM7651CDiPHEC 372-22.5357.154 35,185 1.00 49.66 C C

ATOM7652CD2PHEC 372-21.9675.843 37.108 1.00 50.59 C C

ATOM7653CE1PHEC 372-22.1926.086 34.353 1.00 49.12 G C

ATOM7654CE2PHEC 372-21.6224.768 36.284 1.00 49.07 C C

ATOM7655CZ PHEC 372-21.7344.892 34.903 1.00 49.79 C C

ATOM7656C PHEC 372-25.2527.710 37.399 1.00 53.77 C C

ATOM7657O PHEC 372-25.7287.130 36.415 1.00 54.31 C O
ATOM7658N ILEC 373-25.6327.444 38.645 1.00 54.08 C N

ATOM7659CA ILEC 373-26.6546.439 38.923 1.00 54.72 C C
ATOM7660CB ILEC 373-26.7236.101 40.442 1.00 55.05 C C

ATOM7661CG2ILEC 373-27.9495.239 40.737 1.00 54.76 C C

ATOM7662CG1ILEC 373-25.4495.370 40.875 1.00 54.23 C C
ATOM7663CD1ILEC 373-25.3605.112 42.353 1.00 53.52 C C
ATOM7664C ILEC 373-28.0376.896 38.458 1.00 54.99 C C

ATOM7665O ILEC 373-28.7406.162 37.763 1.00 54.13 C O

ATOM7666N ASPC 374-28.4188.115 38.824 1.00 55.32 C N

ATOM7667CA ASPC 374-29.7328.633 38.457 1.00 56.92 C C

ATOM7668CB ASPC 374-30.008_9.945 39.189 1.00 57.47 C C

ATOM7669CG ASPC 374-30.1799.751 40.677 1.00 58.46 C C

ATOM7670OD1ASPC 374X0.669 8.671 41.080 1.00 59.08 C O

ATOM7671OD2ASPC 374-29.83710.67941.442 1.00 58.58 C O
ATOM7672C ASPC 374-30.0228.828 36.973 1.00 57.69 C C
ATOM76730 ASPC 374-31.1558.611 36.538 1.00 57.47 C O
ATOM7674N TYRC 375-29.0229.233 36.194 1.00 58.43 C N

ATOM7675CA TYRC 375-29.2459.457 34.768 1.00 58.54 C C

ATOM7676CB TYRC 375-25.56710.75834.323 1.00 59.75 C C

ATOM7677CG TYRC 375-29.06311.98135.063 1,00 61.46 C C

ATOM7678CD1TYRC 375-28.39212.45736.186 1.00 61.98 C C

ATOM7679CEiTYRC 375-28.86413.55836.898 1.00 63.16 C C

ATOM7680CD2TYRC 375-30.22812.63934.664 1.00 62.48 C C

ATOM7681CE2TYRC 375-30.71413.74135.370 1.00 63.02 C C

ATOM7682CZ TYRC 375-30.02514.19636.488 1.00 63.61 C C

ATOM7683OH TYRC 375-30.48715.28537.199 1.00 63.54 C O

ATOM7684C TYRC 375-28.8118.318 33.849 1.00 57.88 C C

ATOM7685O TYRC 375-29.2638.233 32.708 1.~ 57.98 C O

ATOM7686N ILEC 376-27.9567.428 34.338 1.00 57.33.C N

ATOM7687CA ILEC 376-27.4976.331 33.497 1.00 56.73 C C

ATOM7688C8 ILEC 37fi-26.0256.562 33.064 1.00 57.40 C C

ATOM7689CG2ILE C 376-25.4595.307 32_.3931.00 56.41 C C
ATOM7690CG7ILE C 376-25,9587.774 32.125 1,00 57.46 C C
ATOM7691CD1ILE C 376-24.5628.130 31.678 1.00 58.58 C C
ATOM7692C ILE C 376-27.6324.922 34.071 1.00 56.17 C C
ATOM7693O ILE C 376-28.3174.075 33.490 1.00 56.10 C O
ATOM7694N VAL C 377-26.9824.666 35.202 1.00 55:46 C N
ATOM7695CA VAL C 377-27.0183.341 35.808 1.00 55.23 C C
ATOM7696CB VAL C 377-26.1143,293 37.065 1.00 55.47 C C

ATOM7697CG1VAL C 377-26.0971.891 37.651 1.00 54.86 C C
ATOM7698CG2VAL C 377-24.6973.724 38.697 1.00 54.49 C C

ATOM7699C VAL C 377-28.4272.851 36.162 1.00 55.80 C C
ATOM77000 VAL C 377-28.8511.791 35.702 1.00 54.91 C O
ATOM7701N . C 378-29.1553.624 36.964 1.00 56.48 C N
HIS

ATOM7702CA HIS C 378x0.501 3,240 37.368 1.00 57.78 C C
ATOM7703CB HIS C -378X1.039 4.213 38,423 1.00 59,01 C C

ATOM7704CG HIS C 378-32.3293.775 39.049 1.00 60.93 C C
ATOM7705CD2HIS C 378-32.5913.222 40.258 1.00 61.10 C C

ATOM7706ND1HIS C 378-33.5413.854 38.395 1.00 61.49 C N

ATOM7707CE1HIS C 37834.492 3,368 39.174 1.00 61.00 C C
ATOM7708NE2HIS C 378-33.9422.977 40.309 1.00 61.02 C N
ATOM7709C HIS C 378-31.4893.131 36,204 1.00 58.61 C C

ATOM771.0O HIS C 378-32.1932.126 36.082 1.00 58.73 C O

ATOM7711N PRO C 379X1.559 4.158 35.334 1.00 58.85 C N

ATOM7712CD PRO C 379-00.8685.459 35.374 1.00 58.37 C C

ATOM7713CA PRO C 379-32.4924.101 34,201 1.00 59.06 C C
ATOM7714CB PRO C 379-32.2125.401 33.456 1.00 58.46 C C

ATOM7715CG PRO C 379-31.7816.328 34.551 1.00 58.18 C C

ATOM7716C PRO C 379-32.2592.871 33.326 1.00 59.87 C C

ATOM7717O PRO C 379-33.1.722.395 32.649 1.00 59.88 C O

ATOM7718N LEU C 380-31.0292.367 33.348 1.00 60.21 C N

ATOM7719CA LEU C 380-30.6581.192 32.569 1.00 60.56 C C

ATOM7720CB LEU C 380-29.1441.974 32.316 1.00 60.01 C C

ATOM7721CG LEU C 380-28.572-0.11731,713 1.00 59.87 C C

ATOM7722CD1LEU C 380-29.207-0.37830.352 1.0D 58.62 C C

ATOM7723CD2LEU C 380-27.055-0.00531.596 1.00 60.17 C C

ATOM7724C LEU C 380-31.055-0.09133.291 1.00 60,89 C C

ATOM7725O LEU C 380X1.775 -0.92832.743 1.00 60.56 C O

ATOM7726N TRP C 38130.573 -0.24534.520 1.00 60.95 C N

ATOM7727CA TRP C 381-30.872-1.43535.303 1.00 61.78 C C

ATOM7728CB TRP C 381-30.059-1.44336.593 1.00 60.23 C C

ATOM7729CG TRP C 381-28.683-1.97936.407 1.00 58.52 C C

ATOM7730CD2TRP C 381-28.307-3.35936.360 1.00 57.91 C C

ATOM7731CE2TRP C 381-26.909-3.40536.197 1.00 56,60 C C

ATOM7732CE3TRP C 381-29,019-4.56536.443 1.00 57.76 C C

ATOM7733CDtTRP C 381-27.533-1.26336.266 1.00 57.34 C C

ATOM7734NE1TRP C 381-26.462-2.11136.142 1.00 56.70 C N

ATOM7735CZ2TRP C 381-26.203-4.60836.118 1.00 56.74 C C

ATOM7736CZ3TRP C 381-28.315-5.76436.365 1.00 57.50 C C

ATOM7737CH2TRP C 381-26.921-5.77536.206 1.00 57.02 C C

ATOM7738C TRP C 381-32.353-1.59435.624 1.00 62.96 C C

ATOM7739O TRP C 381-32.830-2.71335.829 1.00 62.90 C O

ATOM7740N GLU C 382-33.079-0.48135.671 1.00 63.61 C N

ATOM7741CA GLU C 382-34.504-0.54135.945 1.00 84.69 C C

ATOM7742CB GLU C 382-35.1070.863 36.037 1.00 66.09 C C

ATOM7743CG GLU C 382-36.6300.859 36.098 1.00 67.92 C C

ATOM7744CD GLU C 382-37,2252.250 36.127 1.00 68.95 C C

ATOM7745OE1GLU C 382-36.9023.048 35.220 1.00 69.16 C O

ATOM7746OE2GLU C 382-38.0222.540 37.049 1.00 69.15 C O

ATOM7747C GLU C 382-35.152-1.28934.796 1.00 64.47 C C

ATOM7748O GLU C 382-36.068-2.09234.989 1.00 65.29 C O

ATOM7749N THR C 383-34.662-1,02233.593 1.00 63.64 C N

ATOM7750CA THR C 38335.191 -1.66232.404 1.00 63.70 C C

ATOM7751CB THR C 38334.731 -0.92631.129 1.00 63.63 C C

ATOM7752OG1THR C 383-35.0820.462 31.223 1.00 62.90 C O

ATOM7753CG2THR C 383-35.401-1.52029.906 1.00 63.12 C C

ATOM7754C THR C 383-34.759-3.12132.336 1.00 64.19 C C

ATOM7755O THR C 383-35.498-3,96331.829 1.00 64,75 C O

ATOM7756N TRP C 384-33.566-3.42632,844 1.00 64.49 C N

ATOM7757CA TRP C 384X3.084 -4.80332.829 1,00 64.88 C C

ATOM7758CB TRP C 384-31.596-4.87733.186 1.00 63.76 C C

ATOM7759CG TRP C 384-31.067-6.29233.179 1.00 63.50 C C

ATOM7760CD2TRP C 384-30.789-7.09832.024 1.00 63.43 C C

ATOM7761CE2TRP C 38430.382 -8.36932.489 1.00 63.18 C C

ATOM7762CE3TRP C 384-30.848-6,87130.642 1.00 63.29 C C

ATOM7763CDtTRP C 384X0.819 -7.08834.266 1.00 62.59 . C
C

ATOM7764NE1TRP C 384-30.409-$.33533.859 1.00 61.82 C N

ATOM7765CZ2TRP C 384-30.034-9.40931.618 1.00 63.76 C C

ATOM7766CZ3TRP C 384-30.501-7.90629.776 1.00 63.38 C C

ATOM7767CH2TRP C 384-30.100-9.15930.269 1.00 63.69 C C

ATOM7768C TRP C 384-33.892-5.65533.807 1.00 65.86 C C

ATOM7769O TRP C 384-34.204-6.81533.527 1.00 65.93 C O

ATOM7770N ALA C 385-34.229-5.07934.956 1.00 66.87 C N

ATOM7771CA ALA C 385-35.019-5.79435.950 1.00 68.23 C C

ATOM7772CB ALA C 385-35.159-4.95137.206 1.00 67.60 C C

ATOM7773C ALA C 385-36.399-6.11535.367 1.00 69.40 C C

ATOM7774O ALA C 385-36.923-7.21235.553 1.00 69.13 C O

ATOM7775N ASPC 386-36.977-5.158__ 34.6481.00 70.75 C N

ATOM7776CA ASPC 386-38.289-5.350_ 34.0431.00 72.26 C C

ATOM7777CB ASPC 386-38.812-4.02333.503 1.00 73.98 C C

ATOM7778CG ASPC 386-39.249-3.08034.603 1.00 76.49 C C

ATOM7779OD1ASPC 386-38.464-2.86235.557 1.00 77.56 C O

ATOM7780OD2ASPC 386-40.378-2.55334.511 1.00 77.86 C O

ATOM7781C ASPC 386-38.277-6.38332.926 1.00 72.56 C C

ATOM7782O ASPC 386-39.328-6.83832.477 1.00 72.26 C O

ATOM7783N LEUC 387-37.084-6.75032.473 1.00 72.85 C N

ATOM7784CA LEUC 387-36.95_5-7.72931.408 1.00 73.02 C C

ATOM7785CB LEUC 387-35.681-7.46230.598 1.0D 73.39 C C

ATOM7786CG LEUC 387-35.524-8.27429.309 1.00 73.10 C C

ATOM7787CD1LEUG 387-36.583-7.83528.308 1.00 73.12 C C

ATOM7788CD2LEUC 387-34.133-8.07028.728 1.00 73.26 C C

ATOM7789C LEUC 387-36.91_6-9.14331.987 1.00 73.31 C C

ATOM7790O LEUC 387-37.600-10.04231.495 1.00 73.08 C O

ATOM7791N VALC 388-36.110-9.33533.029 1.00 73.28 C N

ATOM7792CA VALC 388-35.986-10.64133.671 1.00 74.00 C C

ATOM7793CB VALC 388-34.502-11.00733.914 1.00 73.32 C C

ATOM7794CG1VALC 388-33.754-11.03132.593 1.00 72.66 C C

ATOM7795CG2VALC 388-33.868-10.01334.873 1.00 72.24 C C
I

ATOM7796C VALC 388-36.723-10.64135.010 1.00 74.81 C C
.

ATOM7797O VALC 388-36.368-11.37835.935 1.00 74.36 C O
~

ATOM7798N HISC 389-37.753-9.80635.094 1.00 75.59 C N

ATOM7799CA HISC 389-38.558-9.67136.299 1.00 76.46 C C

ATOM7800CB HISC 389-39.846-8.91735.969 1.00 77.51 C C

ATOM7801CG HISC 389-40.519-8.32537.166 1.00 79.14 C C

ATOM7802CD2HISC 389-40.893-7.05337.440 1.00 79.52 C C

ATOM7803ND1HISC 389-40.865-9.07538.269 1.00 79.57 C N

ATOM7804CE1HISC 389-41.423-8.28939.173 1.00 80.11 C C

ATOM7805NE2HISC 389-41.452-7.05838.695 1.00 80.49 C N

ATOM7806C HISC 3B9-38.903-11.03336.898 1.00 76.39 C C

ATOM7807O HISC 389-39.506-11.87336.231 1.00 76.45 C O

ATOM7808N PROC 390-38.534-11.26838.171 1.00 76.26 C N

ATOM7809CD PROC 390-39.221-12.32638.938 1.00 76.31 C C

ATOM7810CA PROC 390-37.822-10.37039.087 1.00 76.15 C C

ATOM7811CB PROC 390-38.689-10.42940.324 1.00 76.90 C C

ATOM7812CG PROC 390-38.953-11.92540.401 1.00 76.56 C C

ATOM7813C PROC 390-36.406-10.86039.399 1.00 75.75 C C

ATOM7814O PROC 390-35.871-10.57440.471 1.00 75.54 C O

ATOM7815N ASPC 391-35.806-11.59538.472 1.00 75.05 C N

ATOM7816CA ASPC 391-34.476-12.14238.692 1.00 74.75 C C
.

ATOM7817CB ASPC 391-33.962-12.80637.419 1.00 75.12 C C

ATOM7818CG ASPC 391-34.823-13.96736.979 1.00 75.33 C C

ATOM7819OD1ASPC 391-35.182-14.80237.836 1.00 75.40 C O

ATOM7820OD2ASPC 391-35.131-14.05035.773 1.00 75.66 C O

ATOM7821C ASPC 391-33.419-11.172_39._1971.00 74.44 C C

ATOM7822O ASPC 391-32.399-11.60339_.7261.00 74.60 C O

ATOM7823N ALAC 392-33.651-9.87139.048__1.00 74.27 C N

ATOM7824CA ALAC 392-32.663-8.88739.488 _1_.0074.14 C C
.

ATOM7825CB ALAC 392-32.129-8.12338.280 1.00 74.55 C C

ATOM7826C ALAC 392-33.163-7.89940.532 1.00 73.88 C C

ATOM7827O ALAC 392-32.608-6.8074_0.6691.00 74.19 C O

ATOM7828N GLNC 393-34.198-8.28041.271 1.00 73.33 C N

ATOM7829CA GLNC 393-34.760-7.40342.287 1.00 72.76 C C

ATOM7830CB GLNC 393-35.950-8.08142.968 1.00 73.71 C C

ATOM7831CG GLNC 393-36.651-7.19443.982 1.00 75.45 C C

ATOM7832CD GLNC 393-37.057-5.84843.399 1.00 76.45 C C

ATOM7833OE1GLNC 393-37.871-5.77442.474 1.00 76.51 C O

ATOM7834NE2GLNC 393-36.485-4.77543.938 1.00 76.60 C N

ATOM7835C GLNC 393-33.735-6.97543.338 1.00 71.90 C C

ATOM78360 GLNC 393-33.693-5.81043.729 1.00 71.14 C O

ATOM7837N ASPC 394-32.911-7.90943.797 1.00 71.64 C N

ATOM7838CA ASPC 394-31.904-7.57744.798 1.00 71.60 C C

ATOM7839CB ASPC 394-31.242-8.84445.342 1.00 72.92 C C

ATOM7840CG ASPC 394-32.218-9.73846.083 1.00 74.47 C C

ATOM7841ODtASPC 394-32.886-9.24647,020 1.00 74.84 C O

ATOM7842OD2ASPC 394-32.315-10.93545.732 1.00 75.33 C O

ATOM7843C ASPC 394-30.843-6.64544.223 1.00 71.12 C C

ATOM7844O ASPC 394-30.398-5.71344.896 1.00 71.18 C O

ATOM7845N ILEC 395-30.439-6.89342.979 1.00 69.76 C N

ATOM7846CA ILEC 395-29.436-6.05242.336 1.00 68.39 C C

ATOM7847CB ILEC 395-29.147-6.52640.889 1.00 67.44 C C

ATOM7848CG2ILEC 395-28.252-5.51840.173 1.00 66.84 C C

ATOM7849CG1ILEC 395-28.474-7.90340.923 1.00 66.71 C C

ATOM7850CD1ILEC 395-28.107-8.45539.563 1.00 65.11 C C

ATOM7851C ILEC 395-29.908-4.59942.316 1.00 68.30 C C

ATOM7852O ILEC 395-29.180-3.69342.733 1.00 68.19 C O

ATOM7853N LEUC 396-31.132-4.38141.845 1.00 67.87 C N

ATOM7854CA LEUC 396-31.685-3.03441.780 1.00 67.70 C C

ATOM7855CB LEUC 396-33.085-3.05741.160 1.00 67.99 C C

ATOM7856CG LEUC 396-33.601-1.76840.503 1.00 68.12 C C

ATOM7857CD1LEUC 396-35.058-1.96440.129 1.00 68.21 C C

ATOM7858CD2LEUC 396-33.459-0.57741.435 1.00 68.51 C C

ATOM7859C LEUC 396-31.762-2.45343.185 1.00 67.49 C C

ATOM78600 LEUG 396-31.428-1.28543.398 1.00 68.20 C O

i 7861N ASP 397-32.205-3.26744.141 1.00 66.54 C N
ATOM C

ATOM7862CA ASP 397-32.318-2.81245.520 1.00 66.01 C C
C

ATOM7863CB ASP 397-32.893-3.91946.420 1.00 67.16 C C
C

ATOM7864CG ASP 397-34.397-4.13646.209 1.00 68.46 C C
C

ATOM7865OD1ASP 397-35.157-3.14546.234 1.00 68.68 C O
C

ATOM7866OD2ASP 397-34.825-5.29846.028 1.00 69.00 C O
.
C

ATOM7867C ASP 397-30.952-2.37646.026 1.00 64.63 C C
.
C

ATOM7868O ASP 397-30.822-1.33646.663 1.00 64.23 C O
' C

ATOM7869N THR 398-29.931-3.17245.730 1.00 64.20 C N
C

ATOM7870CA THR 398-28.567-2.85746.151 1.00 63.10 C C
C

ATOM7871CB THR 398-27.566-3.92845.675 1.00 62.67 C C
C

ATOM7872OG1THR 398-28.045-5.22946.031 1.00 62.31 C O
C

ATOM7873CG2THR 398-26.205-3.70346.315 1.00 61.63 C C
C

ATOM7874C THR 398-28.141-1.51745.557 1.00 62.75 C C
C

ATOM7875O THR 398-27.486-0.71146.223 1.00 62.41 C O
C

ATOM7876N LEU 399-28.515-1.28944.300 1.00 62.09 C N
C

ATOM7877CA LEU 399-28.173-0.04843.610 1.00 61.86 C C
C

ATOM7878CB LEU 399-28.618-0.12642.146 1.00 61.59 C C
C

ATOM7879CG LEU 399-28.3211.072 41.234 1.00 61.61 C C
C

ATOM7880CD1LEU 399-26.8251.350 41.203 1.00 60.18 C C
C

ATOM7881CD2LEU 399-28.8400.782 39.829 1.00 60.2D C C
C

ATOM7882C LEU 399-28.8101.170 44.286 1.00 61.66 C C
C

ATOM7883O LEU 399-28.1512.192 44.483 1.00 61.21 C O
C

ATOM7884N GLU 400-30.0871.055 44.646 1.00 61.63 C N
C

ATOM7885CA GLU 400-30.8052.153 45.289 1.00 61.33 C C
C

ATOM7886CB GLU 400-32.2881.806 45.425 1.00 62.10 C C
C

ATOM7887CG GLU 4D0-33.0281.655 44.098 1.00 63.00 C C
C

ATOM7888CD GLU 400-34.4851.242 44.284 1.00 64.29 C C
C

ATOM7889OE1GLU 400-35.2361.208 43.279 1.00 63.16 C O
ATOM7890OE2C 400-34.8790.949 45.439 1.00 64.31 C O
GLU
C

ATOM7891C GLU 400-30.2282.494 46.659 1.00 61.20 C C
C

ATOM7892O GLU 400-30.2763.646 47.088 1.00 60.67 C O
ATOM7893N C 401-29.6751.493 47.340 1.00 60.92 C N
ASP
C

ATOM7894CA ASP 401-29.0831.712 48.656 1.00 61.28 C C
C

ATOM7895CB ASP 401-28.9640.395 49.429 1.00 62.08 C C
ATOM7896CG C 401-30.314-0.23549.714 1.00 63.31 C C
ASP
C

ATOM7897OD1ASP 401-31.3440.464 49.571 1.00 63.51 C O
C

ATOM7898OD2ASP 401-30.346-1.42850.090 1.00 63.73 C O
ATOM7899C C 401-27.7132.363 48.544 1.00 60.58 C C
ATOM7900O ASP 401-27.3153.143 49.410 1.0D 60.44 C O
C
ASP
C

ATOM7901N ASN 402-26.9812 47 1.00 60.06 C N
C .035 .

ATOM7902CA ASN 402_ _ _ 1.00 __ C C
C -25.670_ _ 59.37 2.637 _ _47_280 ATOM7903CB ASN 402-24.9051.912 46_170 1.00 58.07 C C
C

ATOM7904CG ASN 402-24.3590.580 _ 1.00 56.82 C C
C 46.619 ATOM7905ODtASN 402-23.6640.499 47.623 1.00 57.08 C O
C

ATOM7906ND2ASN 402-24.661-0.47145.872 1,00 56.65 C N
C

ATOM7907C ASN 402-25.9084.089 46.888 1.00 59.06 C C
C

ATOM7908O ASN 402-25.1664.988 47.283 1.00 58.71 C O
C

ATOM7909N ARG 403-26.9664.299 46.114 1.0D 59.47 C N
C

ATOM7910CA ARG 403-27.3505.625 45.653 1.00 60.81 C C
C

ATOM7911CB ARG 403-28.6605.519 44.858 1.00 62.02 C C
C

ATOM7912CG ARG 403-29.0966.773 44.109 1.00 63.28 C C
C

ATOM7913CD ARG 403-29.6077.853 45.042 1.00 64.72 C C
C

ATOM7914NE ARG 403-30.1758.976 44.304 1.00 66.85 C N
ATOM7915CZ C 403-30.59210.10644.866 1.00 67.46 C C
ARG
C

ATOM7916NHiARG 403-30.50410.26846.179 1.00 67.95 C N
C

ATOM7917NH2ARG 403-31.09811.07444.116 1.00 68.12 C N
C

ATOM7918C ARG 403-27.5236.548 46.859 1.00 61.26 C C
ATOM79190 C 403-27.0417.681 46.866 1.00 60.43 C O
ARG
C

ATOM7920N GLU 404-28.2056.044 47.884 1.00 62.49 C N
C

ATOM7921CA GLU 404-28.4476.807 49.101 1.00 62.98 C C
C

ATOM7922CB GLU 404-29.5846.170 49.898 1.00 63.58 C C
C

ATOM7923CG GLU 404-3D.9136.226 49.175 1.00 64.89 C C
C

ATOM7924CD GLU 404-31.4167.647 49.016 1.00 65.80 C C
C

ATOM7925OE1GLU 404-32.1857.906 48.063 1.00 65.78 C O
C

ATOM7926OE2GLU 404-31.0488.501 49.856 1.00 66.14 C O
C

ATOM7927C GLU 404-27.2026.899 49.965 1.00 63.52 C C
C

ATOM7928O GLU 404-26.9387.938 50.572 1.00 63.43 C O
C

ATOM7929N TRP 405-26.4295.821 50.027 1.00 63.88 C N
C

ATOM7930CA TRP 405-25.2295.853 50.840 1.00 64.83 C C
C

ATOM7931CB TRP 405-24.4004.583 50.665 1.00 65.43 C C
C

ATOM7932CG TRP 405-23.2454.536 51_.6281.00 66.68 C C
C

ATOM7933CD2TRP 405-21.8944.940 51.370 1.00 66.92 C C
C

ATOM7934CE2TRP 405-21.1774.796 52.580 1.00 67.00 C C
C

ATOM7935CE3TRP 405-21.2205.412 50.235 1.00 66.90 C C
C

ATOM7936CD1TRP 405-23.2894,172 52.945 1.00 67.15 C C
C

ATOM7937NE1TRP 405-22.0524.326 53.523 1.00 66.83 C N
C

ATOM7938C22TRP 405-19.8165.107 52.688 1.00 67.84 C C
C

ATOM7939CZ3TRP 405-19.8645.721 50.343 1.00 67.75 C C
C

ATOM7940CH2TRP 405-19.1795.566 51.562 1.00 67.72 C C
C

ATOM7941C TRP 405-24.3957.058 50.434 1.00 65.44 C C
C

ATOM794_2__O TRP 405-23.9817.846 51.282 1.00 65.48 C O
C

ATOM7943N TYR 406-24.1587.207 49.134 1.00 65.87 C N
C

ATOM7944CA TYR 406-23.3688.332 48.642 1.00 67.34 C C
C

ATOM7945CB TYR 406-23.0478.162 47.148 1.00 65.61 C C
C

~ 7946CG T~'R 406I -21.6807.563 46.889 ~ 1.0063.53 C ~
ATOMI I I I I ~ ~ C
I C
I

ATOM7947GD1TYRC 406-20.5238.238 47.274 1.00 63.28 C C

ATOM7948CEtTYRC 406-19.2667.681 47.079 1.00 62.32 C C

ATOM7949CD2NR C 406-21.5436.311 -- 46.2961.00 62.62 C C

ATOM7950CE2TYRC 406-20.2875.744 46.097 1.00 61.64 C C

ATOM7951CZ TYRC 406-19.1556.433 46.493 1.00 61.93 C C

ATOM7952OH NR C 406-17.9125.870 46.331 1.00 62_.17C O

ATOM7953C TYRC 406-24.0719.663 48.874 1.00 68.59 C C

ATOM7954O TYRC 406-23.42710.66149.204 1.00 68.93 C O

ATOM7955N GLNC 407-25.3899.674 48.701 1,00_ 70.90 C N

ATOM7956CA GLNC 407-26.18010.88648.895 1.00 72.98 C C

ATOM7957CB GLNC 407-27.66410.59948.635 1.00 73.40 C C

ATOM7958CG GLNC 407-28.58911.77848.912 1.00 73.84 C C

ATOM7959CD GLNC 407-28.30412.97248.023 1.00 73.60 C C

ATOM7960OE1GLNC 4D7-28.45912.90346.804 1.00 73.19 C O

ATOM7961NE2GLNC 407-27.88414.07748.632 1.00 73.30 C N

ATOM7962C GLNC 407-26.00511.43550.308 1.00 73.75 C C

ATOM7963O GLNC 407-25.68112.60750.496 1.00 73.91 C O
' ATOM7964N SERC 408-26.21210.58251.302 1.00 75.28 C N

ATOM7965CA SERC 408-26.07710.99652.692 1.00 77.01 C C
.

ATOM7966CB SERC 408-26.5889.891 53.621 1.00 76.75 C C

ATOM7967OG SERC 408-25.8118.713 53.494 1.00 76.61 C O
:

ATOM7968C SERC 408-24.62911.33053.040 1.00 78.26 C C

ATOM7969O SERC 408-24.26511.38954.212 1.00 78.75 C O

ATOM7970N THRC 409-23.80911.54852.018 1.00 79.73 .CN

ATOM7971CA THRC 409-22.40311.87552.213 1.00 81.72 C C

ATOM7972CB THRC 409-21.48510.80451.591 1.00 81.60 C C

ATOM7973OG1THRC 409-21.9959.501 51.890 1.00 81.75 C O

ATOM7974CG2THRC 409-20.06810.92552.143 1.00 82.24 C C

ATOM7975C THRC 409-22.11613.18251.501 1.00 83.15 C C

ATOM7976O THRC 409-20.99513.68451.534 1.00 82.68 C O

ATOM7977N ILEC 410-23.14913.73150.873 1.00 85.20 C N

ATOM7978CA ILEC 410-23.01914.95050.086 1.00 87.57 C C

ATOM7979CB ILEC 410-24.13715.02149.020 1.00 87.55 C C

ATOM7980CG2ILEC 410-24.20416.42645.414 1.00 87.76 C C

ATOM7981CG1ILEC 410-23.87613.97047.937 1.00 87.23 C C

ATOM7982CD1ILEC 410-24.89613.98446.810 1.00 87.08 C C

ATOM7983C ILEC 410-22.94216.31550.770 1.00 89.38 C C

ATOM7984O ILEC 410-23.90016.77651.391 1.00 89.10 C O

ATOM7985N PROC 411-21.76916.96550.670 1.00 91.52 C N

ATOM7986CD PROC 411-20.50016.30150.301 1.00 91.74 C C

ATOM7987CA PROC 411-21.50418.29251.233 1.00 93.26 C C

ATOM7988CB PROC 411-20.03918.20051.642 1.00 92.57 C C

ATOM7989CG PROC 411-19.46317.39350.535 1.00 91.90 C C

ATOM7990C PROC 411-21.74219.24050.041 1.00 95.19 C C

ATOM7991O PROC 411-22.38218.83949.060 1.00 95.80 C O

ATOM7992N GLNC 412-21.24420.47450.098 1.00 96.73 C N

ATOM7993CA GLNC 412-21.45221.39748.976 1.00 97.69 C C
ATOM7994CB GLNC 412-22.84922.03149.076 1.00 98.49 C C
ATOM7995CG GLNC 412-23.26722.83847.845 1.00 99.68 C C

ATOM7996CD GLNC 412-24.77423.05147.765 1.00 100.00C C

ATOM7997OE1GLNC 412-25.39323.57048.699 1.00 100.00C O

ATOM7998NE2GLNC 412-25.37122.64946.641 1.00 99.75 C N
ATOM7999C GLNC 412-20.38522.48648.859 1.00 97.94 C C

ATOM8000O GLNC 412-20.75123.68148.884 1.00 98.16 C O

ATOM8001OXTGLNC 412-19.19222.13048.728 1.00 98.14 C 0 ATOM8002CB ILED 79 4.533 27.370-12.2201.00 86.79 D C

ATOM8003CG2ILED 79 4.654 28.602-13.1131.00 86.68 D C
ATOM8004CG1ILED 79 5.520 27.501-11.05?1.00 86.81 D C

ATOM8005CDiILED 79 5.732 26.225-10.2571.00 86.56 D C
ATOM8006C ILED 79 2.117 27.239-12.8951.00 86.52 D C

ATOM8007O ILED 79 1.490 28.258-13.1841.00 86.42 D O

ATOM8008N ILED 79 2.901 26.026-10.8321.00 86.77 D N

ATOM5009CA ILED 79 3.070 27.235-11.6921.00 86.70 D C

ATOM8010N PROD 80 1.989 26.100-13.6061.00 86.34 D N

ATOM8011CD PROD 80 2.576 24.779-13.3191.00 86.63 D C

ATOM8012CA PROD 80 1.099 26.025-14.7741.00 85.85 D C

ATOM5013CB PROD 80 1.192 24.554-15.1911.00 86.05 D C

ATOM8014CG PROD 80 _1.555_23.850-13.9151.00 86.45 D C

ATOM8015C PROD 80 -0.341 26.493-14.5381.00 85.35 D C

ATOM8016O PROD 80 -0.882 26.375-13.4321.00 85.29 D O

ATOM8017N ARGD 81 -0.943 27.016-15.6051.00 84.28 D N

ATOM8018CA ARGD 81 -2.301 27.565-15.6041.00 83.33 D C

ATOM8019CB ARGD 81 -2.731 27.839-17.0501.00 83.10 D C

ATOM8020CG ARGD 81 -4.067 28.556-17.2001.00 82.75 D C

ATOM8021CD _ARGD 81 X1.327 2_8.902-18.6621.00 82.23 D C
_ ATOMB022NE ARGD 81 -5.638 29.509-18.8701.00 81.69 D N

ATOM8023CZ ARGD 81 -6.128 29.845-_20.0611.00 81.43 D C

ATOM8024NH1ARGD 81 -5.416 29.634-2_1.1601.00 81.12 D N

ATOM8025NH2ARGD 81 -7.336 30.386-20.1561.00 81.05 D N

ATOM8026C ARGD 81 -3,401 26.778-14.8911.00 82.83 D C

ATOM8027O ARGD 81 -4.084 27.317-14.0181.00 82.27 D O

ATOM8028N PHED 82 -3.580 25.514-15.2621.00 82.56 D N

ATOM8029CA PHED 82 -4.627 24.692-14.6571.00 82.45 D C

ATOM8030CB PHED 82 -5.454 24.025-15.7611.00 81.63 D C

ATOM8031CG PHED 82 -6.112 25.005-16.6861.00 81.09 D C

ATOM8032CD1PHED 82 -7.047 25.913-16.2011.00 81.10 D C

ATOM8033CD2PHE D 82-5.783 25.039-18.0361.00 81,41 D C

ATOM8034CE7PHE D 82-7.644 26.840-17.0441.00 81.01 D C
ATOM8035CE2PHE D 82-6.375 25.966-18.8901.00 80.94 D C

ATOM8036CZ PHE D 82-7.307 26.867-.18.3901.00 80.97 D C
ATOM8037C PHE D 82-4.138 23,639-13.6611.00 82.39 D C

ATOM8038O PHE D 82-4.726 22.561-13.5471.00 82.48 D O

ATOM8039N GLY D 83-3.071 23.960-12.93fi1.00 82.23 D N

ATOM8040CA GLY D 83-2.544 23,032-11.9551.00 $1.88 D C

ATOM8041C GLY D 83-1.442 22.132-12.4691.00 82.12 D C

ATOM8042O GLY D 83-0.446 21,925-11.7781.00 82.61 D O

ATOM8043N VAL D 84-1.608 21,598-13.6771.00 82.26 D N

ATOM8044CA VAL D 84-0.609 20.703-14.2621.00 82.36 D C
ATOM8045CB VAL D 84-1.207 19.285-14.4721.00 82.35 D C

ATOM8046CG1VAL I 84-0.101 18.275-14.7711.00 83.56 D C
D

ATOM8047CG2VAL ' 84-1.967 18.865-13.2321.00 82.72 D C
ATOM8048C VAL D 84-0.066 21.227-15.5991.00 81.82 D C
' D

ATOM8049O VAL D 84-0.536 22.240-16.1161.00 81.45 D O

ATOM8050N LYS D 850.936 20,540-16.1421.00 81.72 D N

ATOM8051CA LYS D 851.539 20.922-17.4161.00 81,88 D C

ATOM8052CB LYS D 853.022 20.541-17.4461.00 81.32 D C

ATOM8053CG LYS D 853.828 21.050-16.2611.00 82.51 D C

ATOM8054CD LYS D 855.243 20.472-16.2581.00 82.79 D C

ATOM8055CE LYS D 856.003 20;850-14.9931.00 82.39 D C
' ATOM8056NZ LYS D 857,417 20.387-15.0361.00 82.13 D N
ATOM8057C LYS D 850.813 20.199-18.5481.00 82.14 D C

ATOM8058O LYS D 850.536 19.001-18.4531.00 81.95 D O

ATOM8059N THR D 860.509 20.933-19.6141.00 82.66 D N

ATOM8060CA THR D 86-0.180 20.374-20.7761.00 82.87 D C
ATOM8061CB THR D 86-1.712 20.271-20.5151.00 82.45 D C

ATOM8062OG1THR D 86-2.376 19.832-21.7091.00 82.02 D O

ATOM8063CG2THR D 86-2.281 21.615-20.0821.00 81,65 D C

ATOM8064C THR D 860.084 21.245-22.0111.00 83.27 D C

ATOM8065O THR D 860.065 22.477-21.9261.00 83.44 D O

ATOM8066N GLU D 870.348 20.605-23.1501.00 83.47 D N

ATOM8067CA GLU D 87O.6i 21,333-24.3911.00 83,79 D C

ATOM8068CB GLU D 871.600 20.546-25.2661.00 84,34 D C

ATOM8069CG GLU D 871.202 19.106-25.5381.00 86.03 D C

ATOM8070CD GLU D 872.286 18.329-26.2721.00 87.11 D C

ATOM8071OE1GLU D 872.708 18.765-27.3681.00 87.53 D 0 ATOM8072OE2GLU D 872.718 17,277-25.7521.00 87.57 D O

ATOM8073C GLU D 87-0.686 21.631-25.1551.00 83.28 D C

ATOM8074O GLU D 87-0.700 22.412-26.1081.00 83.49 D O

ATOM8075N GLN D 88-1.771 20.998-24.7151.00 82.51 D N

ATOM8076CA GLN D 88-3.103 21,180-25.2911.00 81.12 D C

ATOM8077CB GLN D 88-3.840 19.840-25.3451.00 81.83 D C

ATOM8078CG GLN D 88-3.437 18.921-26.4741.00 81.93 D C

ATOM8079CD GLN D 88-4.235 19,186-27.7301.00 82.58 D C

ATOM8080OEiGLN D 88-4.199 20.286-28.2841.00 83.04 D O

ATOM8081NE2GLN D 88-4.972 18,178-28.1841.00 82.64 D N

ATOM8082C GLN D 88-3.861 22.118-24.3511.00 80.15 D C

ATOM8083O GLN D 88-5.089 22.074-24.2651.00 79.70 D O

ATOM8084N GLU D 89-3.116 22.963-23.6451.00 78,86 D N

ATOM8085CA GLU D 893.691 23,887-22.6761.00 77.76 D C

ATOM8086CB GLU D 89-2.622 24.862-22.1901.00 78.49 D C

ATOM8087CG GLU D 89-2.854 25.349-20.7701.00 _ D C
80.18 ATOM8088CD GLU D 89-1.668 26.114-20.2151.00 81.00 D C

ATOM8089OE1GLU D 89-1.399 27.235-20.7081.00 _ D O
81.15 ATOM5090OE2GLU D 89-1.003 25.589-19.2911.00 81.00 D O

ATOM8091C GLU D 89-4.905 24.863-23.1771.00 76.38 D C

ATOM8092O GLU D 89-5.860 24.873-22.4261.00 76.62 D 0 ATOM8093N ASP D 90x.863 25,089-24.4371.00 74.35 D N

ATOM8094CA ASP D 905.962 25.836-25.0381.00 71.49 D C

ATOM8095CB ASP D 90-5.709 26.062-26.5331.00 73.36 D C

ATOM8096CG ASP D 90-4.679 27.131-26.7911.00 74.94 D C

ATOM8097OD1ASP D 90-4.921 28.292-28.3961.00 75.61 D O

ATOM8098OD2ASP D 903.630 26.810-27.3921.00 76,14 D O

ATOM8099C ASP D 90-7.286 25.111-2 1.00 _ D C
4.883 68.88 ATOM8100O ASP D 90-8.227 25.647_ 1.00 68.77 D O
-24.307 ATOM8101N VAL D 91-7.348 23.890-25.4081.00 65.77 D N

ATOM8102CA VAL D 91-8.563 23.084-25.3461.00 63.28 D C

ATOM8103CB VAL D 91-8.399 21.763-26.1211.00 63.41 D C

ATOM8104CG1VAL D 91-9.721 20.999-26.1321.00 63.43 D C

ATOM8105CG2VAL D 91-7.939 22.052-27.5401.00 63.73 D C

ATOM8106C VAL D 91-8.983 22.759-23.9171.00 61.15 D C

ATOM8107O VAL D 91-10.17822,707-23.6191.00 61.41 D O

ATOM8108N LEU D 92-8.008 22.536-23.0401.00 57.81 D N

ATOM8109CA LEU D 92-8.301 22.227-21.6471.00 55.19 D C

ATOM8110CB LEU D 92-7.014 21.943-20.8661.00 52.82 D C

ATOM8111CG lEU D 92-7.067 20.951-19.6951.00 50.63 D C

ATOM8112CD1LEU D 92-5.925 21.263-18.7511.00 49.21 D C

ATOM8113CD2LEU D 92-8.394 21.019-18.9631.00 47.96 D C

ATOM8114C LEU D 92-8.985 23.445-21.0441.00 54.72 D C

ATOM8115O LEU D 92-9.916 23.325-20.2471.00 54.22 O O

ATOM8116N ALA D 93-8.511 24.619-21.4431.00 54.21 D N

ATOM8117CA ALA D 93-9.045 25.877-20.9511.00 54.48 D C

ATOM8118CB ALA D 93-8.230 27.037-21.4901.00 55.68 D C

ATOM8119C ALAD 93 -10.49326.065-21.3261.00 54.76 D C

ATOM8120O ALAD 93 - -11.29326.514-20.5111.00 54.99 D 0 ATOM8121N LYSD 94 -10.83325.732-22.5641.00 55.52 D N

ATOM8122CA LYSD 94 -12.20425.891-23.0221.00 56.61 D C

ATOM8123CB LYSD 94 -12.28025.785-24.5491.00 58.71 D C

ATOM8124CG LYSD 94 -11.34826.749-25.2661.00 61.94 D C
~

ATOM8125CD LYSD 94 -11.45428.166-24.7181.0D 63.70 D C

ATOM8126CE LYSD 94 -10.30029.036-25.1271.00_ 64.45 D C

ATOM8127NZ LYSD 94 -10.39330.404-24.5371.00 65.11 D N

ATOM8128C LYSD 94 -13.10324.851-22.3821.00 55.79 D C

ATOM8129O LYSD 94 -14.26925.118-22.0961.00 _ D O
___56.21 ATOM8130N GLUD 95 -12.55923.663-22.1521.00 54.45 O N
ATOM8131CA GLUD 95 -13.34722.610-21.5411.00 53.51 D C

ATOM8132CB GLUD 95 -12.58321.282-21.5551.00 54.48 D C

ATOM8133CG GLUD 95 -12.49720.623-22.9151.00 55.56 D C

ATOM8134CD GLUD 95 -13.85720.431-23.5531,00 56.29 D C

ATOM8135OE1GLU' 95 -14.76119.891-22.8781.00 55.93 D O
D

ATOM8136OE2GLU~ 95 -14.01820.818-24.7331.00 57.09 D O
D

ATOM8137C GLUD 95 -13.69722.985-20.1091.00 51.64 D C

ATOM8138O GLU: 95 -14.84722.875-19.8991.00 51.71 D O
D

ATOM8139N. LEU' 96 -12.70423.444-19.3591.00 49.45 D N
D

ATOM8140CA LEUI 96 -12.92123.806-17.9691.00 48.16 D C
D

ATOM8141CB LEUD 96 -11.58024.065-17.2891.00 46.67 D C

ATOM8142CG LEUD 96 -10.74422.795-17.1051.00 44.86 D C

ATOM8143CD1LEUD 96 -_9.36423.170-16.6121.00 43.94 D C
.

ATOM8144CD2LEUD 96 -11.44821.846-16.1311.00 42.74 D C

ATOM8145C LEUD 96 -13.85724.985-17._7661.00 48.03 D C

ATOM8146O LEUD 96 -14.22325,308-16 1,00 46.37 D O
.637 ATOM8147N GLUD 97 -14.24825.629_ 1.00 48.68 D N
-18.859 ATOM8148CA GLUD 97 -15.17026.746-18.7611.00 48.78 D C

ATOM8149CB GLUD 97 -15.28327.470-20.1051.00 50.98 D C

ATOM8150CG GLUD 97 -14.25228,585-20.2751.00 55.61 D C

ATOM8151CD GLUD 97 -14.36029.302-21.6151.00 58.55 D C

ATOM8152OE1GLUD 97 -15.48029.738-21.9761.0D 59.24 D O

ATOM8153OE2GLUD 97 -13.32029.438-22.3031.00 60.20 D O

ATOM8154C GLUD 97 -16.53826.232-18.3121.00 47.44 D C

ATOM8155O GLUD 97 -17.29126.954-17.6571.00 48.58 D O

ATOM8156N ASPD 98 -16.85224.983-18.6481.00 43.83 D N

ATOM8157CA ASPD 98 -18.13124.393-18.2591.00 42.11 D C

ATOM8158CB ASPD 98 -18.56223,336-19.2821.00 44.42 D C

ATOM8159CG ASPD 98 -18.85423.931-20.6571.00 47.18 D C

ATOM8160OD1ASPD 98 -19.48525.014-20.7151.00 47.93 D O

ATOM8161OD2ASPD 98 -18.46623.308-21.6741.00 48.36 D O

ATOM8162C ASPD 98 -18.08323.748-16.8701,00 38.77 D C

ATOM8163O ASPD 98 -18.93122,930-16.5281.00 36.88 D O

ATOM8164N VALD 99 -17.10324.136-16.0651.00 36.12 D N

ATOM8165CA VALD 99 -16.94323.549-14.7481.00 33.89 D C

ATOM8166CB VALD 99 -15.681__24.095-14.0451.00 33.36 D C

ATOM8167CG1VALD 99 -15.93825.608-13.5091.00 32.85 D C

ATOM8168CG2VALD 99 -15.27123.154-12.9371.00 31.96 D C

ATOM8169C VALD 99 -18.15023.754-13.8401.00 33.38 D C

ATOM8170O VALD 99 -18.35122.990-12.9011.00 33.33 D O

ATOM8171N ASND 100-18.95124.776-14.1231.00 31.39 D N

ATOM8172CA ASND 100-20.13725.057-13.3251.00 32.09 D C

ATOM8173CB ASND 100-20.35526.567-13.1751.00 33.27 D C

ATOM8174CG ASND 100-19.13527.285-12.6381.00 34.55 D C

ATOM8175OD1ASND 100-18.51926.864-11.6421.00 32.87 D O

ATOM8176ND2ASND 100-18.77928.385-13.2901.00 35.71 D N

ATOM8177C ASND 100-21.38824.455-13.9531.00 31.24 D C

ATOM8178O ASND 100-22.50624.722-13.5121.00 30.37 D O

ATOM8179N LYSD 101-21.21423.647-14.9861.00 30.50 D N

ATOM8180CA LYSD 101-22.38423.059-15.6201.00 31.69 D C

ATOM8181CB LYSD 101-22.43323.434-17.0991.00 31.66 D C

ATOM8182CG LYSD 101-22.69824,909-17.3561.00 35.28 D C

ATOM8183CD LYSD 101-22.79225.173-18.8521.00 38.50 D C

ATOM8184CE LYSD 101-22.28626.558-19.2221.00 40.55 D C

ATOM8185NZ LYSD 101-21.87526.584-20.6701.00 43.99 D N

ATOM8186C LYSD 101-22.47921.554-15.4851.00 30.64 D C

ATOM8187O LYSD 101-21.47520.845-15.4841.00 29.55 D O

ATOM8188N TRPD 102-23.71221.082-15.3681.00 31.69 D N

ATOM8189CA TRPD 102-23.99619.663-15.2611.00 32.10 D C

ATOM8190CB TRPD 102-25.46119.479-14.8611.00 32.15 D C

ATOM8191CG TRPD 102-25.79615.137-14.2641.00 32.96 D C

ATOM8192CD2TRPD 102-25.53517.706-12.9211.00 30.91 D C

ATOM8193CE2TRPD 102-26.05716.405-12.7951.0D 31.40 D C
ATOM8194CE3TRPD 102-24.90818.293-11.8161.00 30.45 D C
-ATOM8195CD1TRPD 102-26.44227.103-14.8771.00 31 D C

19 ATOM8196NE1TRPD 102-26.60396.062-14.0021.00 . D N

ATOM8197CZ2TRPD 102-25.97215.678-11.6011.00 . D C

ATOM8198CZ3TRPD 102-24.82217.569-10.6311.00 . D C

ATOM8199CH2TRPD 102-25.35216.279-10.5351.00 . D C
29.64 ATOM8200C TRPD 102-23.72719.116-16.6631.00 32.61 D C

ATOM8201O TRPD 102-24.23619.651-17.6461.00 35 D O

ATOM8202N GLYD 103-22.90418.081-16.7661.00 . D N
31:48 ATOM8203CA GLYD 103-22.60617.524-18.0731.00 30.29 D C

ATOM8204C GLYD 103-21.19517.803-18.5761.00 30.35 D C

ATOM8205O GLY D 103-20.89917.583-19.7481.00 31.01 D O

ATOM8206N lEU D 104-20.32418.302-17.7041.00 _ D N
30.64 ATOM8207CA LEU D 10418.937 18.585_ -18.0761.00 30.46 D C

ATOM8208CB LEU D 104-18.12218.879-16.8121.00 28.43 D C

ATOM8209CG LEU D 104-16.59518.953-16.9451.00 30.41 D C
ATOM8210CD1LEU D 104-16.20920.267-17.6391.00 29.60 D C

ATOM5211CD2LEU D 104-15.93518.872-15.5571.00 27.91 D C

ATOM8212C LEU 0 104-18.34517.365-18.7961.00 30.87 D C

ATOM8213O LEU D 104-18.65816.225-18.4471.00 30.75 D O

ATOM8214N HIS D 105-17.50617.603-19.8011.00 31.64 D N

ATOM8215CA HIS D 105-16.85416.511-20.5441.00 32.86 D C

ATOM8216CB HIS D 105-16.38716.999-21.9221.00 34.25 D C

ATOM8217CG HIS D 105-17.47017.632-22.7411.00 38.23 D C

ATOM8215CD2HIS D 105-18.81517.467-22.7291.00 39.85 D C

ATOM8219ND1HIS D 105-17.21018.568-23.7211.00 40.53 D N

ATOM8220CE1HIS D 105-18.34818.952-24.2751.00 40.42 D C

ATOM8221NE2HIS D 105-19.33718.299-23.6921.00 39.93 D N

ATOM8222C HIS D 105-15.64316.068-19.7231.00 32.71 D C

ATOM8223O HIS D 105-14.49716.341-20.0891.00 33.65 D O

ATOM8224N VAL D 106-15.91175.390-18.8091.00 32.42 D N

ATOM8225CA VAL D 106-14.86914.932-17.7031.0D 31.29 D C

ATOM8226C8 VAL D 106-15.48814.346-16.3831.00 31.38 D C

ATOM8227CG1VAL D 106-16.13612.977-16.6321.00 29.70 D C

ATOM8228CG2VAL D 106-14.41214.256-15.3021.00 29.13 D C

ATOM8229C VAL D 106-13.88813.938-18.3231.00 31.28 D C

ATOM8230O VAL D 106-12.69913.977-18.0171.00 31.60 D O

ATOM8231N PHE D 107-14.36113.055-19.1931.00 32.60 O N

ATOM8232CA PHE D 107-13.44812.099-19.8311.00 34.71 D C

ATOM8233CB PHE D 107-14.23411.066-20.6381.00 33.95 D C

ATOM8234CG PHE D 107-14.95410.072-19.7821.00 34.73 D C

ATOM8235CDtPHE D 107-14.2469.079 -19.1061.00 34.63 D C

ATOM8236CD2PHE D 107-16.32810.175-19.5761.00 34.05 D C

ATOM8237CE1PHE D 107-14.8988.210 -18.2341.00 33.36 D C

ATOM8238CE2PHE D 107-16.9859.311 -18.7071.00 32.78 D C

ATOM8239CZ PHE D 107-16.2738.331 -18.0371.00 32.90 D C

ATOM8240C PHE D 107-12.45712.539-20.7321.00 35.60 D C

ATOM8241O PHE D 107-11.27012.512-20.7781.00 35.67 D O

ATOM8242N ARG D 108-12.96113.854-21.4261.00 36.60 D N

ATOM8243CA ARG D 108-12.15214.669-22.3151.00 37.2 D C

ATOM8244CB ARG D 108-13.07115.602-23,1231-.00 _ D C
3_9.4_2 ATOM8245CG ARG D 108-12.38016.515-24.1211.00 42.77 D C

ATOM8246CD ARG D 108-11.56915.730-25.1331.00 46.88 D C

ATOM8247NE ARG D 108-10.95116.609-26.1261.00 51.42 D N

ATOM8248CZ ARG D 108-9.892 16.284-26,8651.00 52.42 D C

ATOM8249NH1ARG D 108-9.318 15-092-26,7301.00 51.60 D N

ATOM8250NH2ARG D 108-9.408 17.154-2 1.00 52.77 D N
7.744 ATOM8251C ARG D 108-11.14315.465_ 1.00 36.70 D C
-21.477 ATOM8252O ARG D 108-9.985 15.606-21.8581.00 35.29 D O

ATOM8253N 1LE D 109-11.57115.985-20.3321.00 36.62 D N

ATOM8254CA ILE D 109-10.65416.731-19.4791.00 36.91 D C

ATOM5255CB tLE D 109-11.39717.426-18.3391.00 36.01 D C

ATOM8256CG2ILE D 109-10.42317.881-17.2651.00 33.76 D C

ATOM8257CG1ILE D 109-12.1_8318.606-18.9181.00 35.38 D C

ATOM8258CD1ILE D 109-13.00119.332-17.9 1.00 35.72 D C

ATOM8259C ILE D 109-9.588 15.789_ 1.00 35.52 D C
-18.924 ATOM8260O ILE D 109-8.440 16.177-18.7231.00 35.45 D O

ATOM8261N ALA D 110-9.969 14.542-18.7031.00 35.61 D N

ATOM8262CA ALA D 110-9.037 13.539-18.2021.00 36.23 D C

ATOM8263CB ALA D 110-9.785 12.245-17.8861.00 35.19 D C

ATOM8264C ALA D 110-7.945 13.279-19.2471.00 37.10 D C

ATOM8265O ALA D 110-6.776 13.112-18.9001.00 36.01 D O

ATOM8266N GLU D 111-8.319 _13.242-20.5281.00 38.59 D N

ATOM8267CA GLU D 111-7.328 13.018-21,5891.00 39.66 D C

ATOM8268CB GLU D 111-8.014 12.642-22.8981.00 42.81 D C

ATOM8269CG GLU D 111-9.047 11.541-22.7501.00 47.43 D C

ATOM8270CD GLU D 111-9.502 10.980-24.0831.00 49.22 D C

ATOM8271OE1GLU D 111-9.816 11.778-25.0051.00 49.33 D O

ATOM8272OE2GLU D 117-9.549 9.733 -24.1931.00 50.73 D O

ATOM8273C GLU D 111-6.453 14.256-21,8151.00 38.59 D C

ATOM8274O GLU D 1115.244 14.149-21.9311.00 38.30 D O

ATOM8275N LEU D 112-7.070 _15.430-21.8531.00 37.66 D N

ATOM8276CA LEU D 112-6.345 16.671-22.0681.00 37.30 D C

ATOM8277C8 LEU D 1 -7.335 17.810-22.2741.00 37.59 D C
i2 ATOM8278CG LEU D 112-8.328 17.570-23.4121.00 39.30 D C

ATOM8279CD1LEU D 112-9.390 _18.671-23.4251.00 38.20 D C

ATOM8280CD2LEU D 112-7.568 17.520-24.7321.00 39.70 D C

ATOM8281C LEU D 112-5.411 17.021-20.9181.00 37.26 D C

ATOM8282O LEU D 112-4.346 17.612-21.1261.00 37.54 D O

ATOM8283N SER D 113-5.808 ___16.661-19.7011.00 35.41 D N

ATOM8284CA SER D 113-4.995 16.969-18.5261.00 33.55 D C

ATOM8285CB SER D 113-5.871 16.988-17.2701.00 32.75 D C

ATOM5286OG SER D 113-6.273 15.668-16.9301.00 28.28 D O

ATOM8287C SER D 113-3.863 15.969-18.3171.00 32.63 0 C

ATOM.8288O SER D 113-3.065 16.126-17.4091.00 31.59 D O

ATOM8289N GLY D 114-3.806 14.937-19.1491.00 33.27 D N

ATOM8290CA GLY D 114-2.775 13.928-18.9911.00 33.07 D C

ATOM8291C GLYD 114-3.120 13.008-17.8341.00 34.09 D C

ATOM8292O GLYD 114-2.241 12.591-17.0711.00 34.91 D O

ATOM8293N ASND 115-4.410 12.702-17.7051.00 33.65 D N

ATOM8294CA ASND 115-4.938 11.832-16.6531.00 33.85 D C

ATOM8295CB ASND 115-4.159 10.512-16.6271.00 36.77 D C

ATOM8296CG ASND 115-4.739 9.504 -15.6511.00 40.92 D C

ATOM8297OD1ASND 115-5.952 9.267 -15.6241.00 42.29 D O

ATOM8298ND2ASND 115-3.870 8.895 -14.8441.00 41.94 D N

ATOM8299C ASND 115-4.921 12.499-15.2721.00 31.78 D C

ATOM8300O ASND 115-4.791 11.832-14.2461.00 33.29 D O

ATOM8301N ARGD 116-5.056 13.819-15.2621.00 29.79 D N

ATOM8302CA ARGD 116-5.087 14.608-14.0371.00 29.32 D C

ATOM8303CB ARGD 116-3.957 15.645-14.0571.00 32.72 D C

ATOM8304CG ARGD 116-2.552 15.093-13.8141.00 35.19 D C

ATOM8305CD ARGD 116-2.406 14.651-12.3851.00 40.43 D C

ATOM8306NE ARGD 116-1.134 13,991-12.1151:00 42.89 D N

ATOM8307CZ ARGD 116-0.898 13.277-11.0201.00 43.68 D C

ATOM8308NH1ARGD 116-1.857 13.141-10.1111.00 45.30 D N

ATOM8309NH2ARGD 1160.285 12.708-10.8281.00 43.19 D N

ATOM8310C ARGD 116-6.441 15.339-13.8801.00 27.83 D C

ATOM8311O ARGD 116-6.484 16.502-13.4571.00 27.10 D 0 ATOM8312N PROD 117-7.562 14.660-14.1901.00 26.16 D N

ATOM8313CD PROD 117-7.718 13.238-14.5471.00 26.90 D C

ATOM8314CA PROD 117-8.876 15.299-14.0701.00 26.27 D C

ATOM8315CB PROD 117-9.836 14.214-14.5541.00 26.55 D C

ATOM8316CG PROD 117-9.156 12.957-14.1511.00 25.37 D C

ATOM8317C PROD 117-9.230 15.788-12.6711.00 26,74 D C

ATOM8318O PROD 117-9.876 16.839-12.5161.00 25.52 D O

ATOM8319N LEUD 118-8.806 15.027-11.6591.00 24.30 D N

ATOM8320CA LEUD 118-9.096 15.378-10.2841.00 23.99 D C

ATOM8321CB LEUD 118-8.852 14.175-9.367 1.00 23.02 D C

ATOM8322CG LEUD 118-9.042 14.482-7.885 1.00 23.69 D C
~

ATOM8323CD1LEUD 118-10.45714.990-7.638 1.00 23.47 D C

ATOM8324CD2LEUD 118-8.776 13.226-7.072 1.00 25.82 D C

ATOM8325C LEUi 118-8.269 16.572-9.829 1.00 23.64 D C
D

ATOM83260 LEU: 118-8.765 17.461-9.142 1.00 23.45 D O
D

ATOM8327N THRD 119-7.002 16.598-10.2121.00 23.67 D N

ATOM8328CA THRD 119-6.135 17.708-9.827 1.00 24.64 D C

ATOM8329CB THRD 119-4.674 17.440-10.2631.00 24.65 D C

ATOM8330OG1THRD 119-4.153 16.340-9.513 1.00 27.59 D O

ATOM8331CG2THRD 119-3.799 18.649-10.0311.00 21.49 D C

ATOM8332C THRD 119-6.609 19.008-10.4691.00 25.33 D C

ATOM8333O THRD 119-6.777 20.020-9.792 1.00 28.27 D O

ATOM8334N VALD 120-6.837 18.963-11.7781.00 25.45 D N

ATOM8335CA VALD 120-7.269 20.128-12.5501.00 25.49 D C

ATOM8336CB VALD 120-7.207 19.802-14.0711.00 26.00 D C

ATOM8337CG1VALD 120-7.869 20.880-14.8801.00 26.49 D C

ATOM8338CG2VALD 120-5.739 19.644-14,4911.00 24.26 D C

ATOM8339C VALD 120-8.650 20.640-12.1521.00 24.72 D C

ATOM83400 VALD 120-8.834 21.836-11.9571.00 26,28 D O

ATOM8341N ILED 121-9.619 19.750-12.0011.00 25.15 D N

ATOM8342CA ILED 121-10.95920.191-11.6061.00 25.72 D C

ATOM8343CB ILED 121-11.99019.052-11.7641.00 27.05 D C

ATOM8344CG2ILED 121-13.28419.376-11.0241.00 27.97 D C

ATOM8345CG1ILED 121-12.25318.853-13.2861.0D 27.81 D C

ATOM8346CD1ILED 121-13.09917.626-13.6311.00 28.26 D C

ATOM8347C ILED 121-10.98120.728-10.1711.0D 23.83 D C

ATOM8348O ILED 121-11.62621.725-9.894 1.00 24.54 D O

ATOM8349N METD 122-10.25620.086-9.261 1.00 24.00 D N

ATOM8350CA METD 122-10.19920.574-7.883 1.00 23.21 D C

ATOM8351CB METD 122-9.440 19.584-6.994 1.00 21.50 D C

ATOM8352CG METD 122-10.28818.403-6.530 1.00 22.71 D C

ATOM8353SD METD 122-11.48318.897-5.234 1.00 23.37 D S

ATOM8354CE METD 122-10.38418.981-3.824 1.00 19.99 D C

ATOM8355C METD 122-9.531 21.952-7.853 1.00 22.69 D C

ATOM8356O METD 122-10.01222.876-7.203 1.00 21.45 D O

ATOM8357N HISD 123-8.428 22.094-8.580 1.00 24.16 D N

ATOM8358CA HISD 123-7.723 23.369-8.630 1.00 26.01 D C

ATOM8359CB HISD 123-6.507 23.259-9.549 1.00 29.46 D C

ATOM8360CG HISD 123-5.741 24.534-9.687 1.00 32.24 D C

ATOM8361CD2HISD 123-5.537 25.341-10.7561.04 35.01 D C

ATOM8362ND1HISD 123-5.058 25.107-8.637 1.00 34.59 D N

ATOM8363CE1HISD 123-4.461 26.210-9.050 1.00 35.62 D C

ATOM8364NE2HISD 123x.735 26.374-10.3341.00 37.98 D N

ATOM8365C HISD 123-8.650 24.463-9.158 1.00 25.72 D C

ATOM8366O HISD 123-8.717 25.556-8.598 1.00 26.25 D O

ATOM8367N THRD 124-9.363 24.162-10.2411.00 25.88 D N

ATOM8368CA THRD 124-10.28225.122-10.8411.00 26.60 D C

ATOM8369CB THRD 124-10.93624.523-12.0981.00 28.29 D C

ATOM8370OG1THRD 124-9.910 24.191-13.0371.00 31.57 D 0 _ ATOM8371CG2THRD 124-11.91025.513_ 1.00 29.25 D C
_12.744 ATOM8372C THRD 124-11.36925.543-9.838 1.00 25.49 D C

ATOM8373O THRD 124-11.62526.727-9.656 1.00 24.73 D O

ATOM5374N ILED 125-11.96424.569-9.174 1.00 24.70 D N

ATOM8375CA ILED 125-12.99824.853-8.191 1.00 24.47 D C

ATOM8376CB ILED 125-13.65023.522-7.704 1.00 24.96 D C

ATOM 8377CG2ILED 125-14.59923.7876.534 1.00 25.05 DC

ATOM $378CG1ILED 125-14.37122.858-8.8891.00 24.83 DC

ATOM 8379CD1ILED 125-15.16521.635-8.5511.00 25.61 DC

ATOM 8380C ILED 125-12.46325.672-7.0051.00 26.06 DC

ATOM 8381O ILED 125-13.10526.628-6.5651.00 27.65 DO

ATOM 8382N PHED 126-11.29325.316-6.4791.00 26.09 DN

ATOM 8383CA PHED 126-10.73426.085-5.3691.00 25.62 DC

ATOM 8384CB PHED 126-9.458 25.418-4.8311.00 25.69 DC

ATOM 8385CG PHED 126-9.708 24.338-3.8011.00 24.53 DC

ATOM 8386CD1PHED 126-10.49323.230-4.1021.00 25.86 DC

ATOM $387CD2PHED 126-9.152 24.431-2.5311.00 24.45 DC

ATOM 8388CE1PHED 126-10.72422.230-3.1551.00 23.16 DC

ATOM 8389CE2PHED 126-9.376 23.433-1.5751.00 24.18 DC

ATOM 8390CZ PHED 126-10.16322.335-1.8911.00 22.74 DC

ATOM 8391C PHED 126-10.43027.538-5.7871.00 26.33 DC

ATOM 8392O PHED 126-10.64828.468-5.0011.00 26.37 DO

ATOM 8393N GLND 127-9.926 27.746-7.0041.00 26.77 DN

ATOM 8394CA GLND 127-9.637 29.116-7.4551.00 30.33 DC

ATOM 8395CB GLN, 127-8.871 29.138-8.7911.00 30.90 DC
D

ATOM 8396CG GLNI 127-7.410 28.700-8.7401.00 33.90 DC
D

ATOM 8397CD GLNI 127-6.498 29.673-7.9831.00 35.88 0C
D

ATOM 8398OE1GLN. 127-5.273 29.501-7.9661.00 36.74 DO
D

ATOM 8399NE2GLND 127-7.087 30.684-7.3531.00 34.82 DN

ATOM 8400C GLND 127-10.96029.846-7.6561.00 30.27 DC

ATOM 8401O GLND 127-11.15730.965-7.1981.00 32.02 DO

ATOM 8402N GLUD 128-11.87029.191-8.3461.00 29.31 DN

ATOM 8403CA GLUD 128-13.16229.775-8.6131.00 30.86 DC

ATOM 8404CB GLUD 128-13.98128.790-9.4451.00 33.63 DC

ATOM 8405CG GLUD 128-15.42829.166-9.6051.00 43.00 DC

ATOM 8406CD GLUD 128-15.83229.221-11.0591.00 47.54 DC

ATOM 8407OE1GLUD 128-15.66928.185-11.7501.00 49.93 DO

ATOM 8408OE2GLUD 128-16.30330.297-11.5051.00 48.$5 DO

ATOM 8409C GLUD 128-13.91430.172-7.3331.00 30.31 DC

ATOM 8410O GLUD 128-14.51731.247-7.2791.00 29.70 DO

ATOM 8411N ARGD 129-13.87529.321-6.3021.00 28.48 DN

ATOM 8412CA ARGD 129-14.57429.624-5.0401.00 27.48 DC

ATOM 8413CB ARGD 129-15.05528.335-4.3561.00 25.54 DC

ATOM 8414CG ARGD 129-16.26427.701-5.0071.00 26.38 DC

ATOM 8415CD ARGD 129-16.58426.344-4.4071.00 27.04 DC

ATOM 8416NE ARGD 129-17.76225.776-5.0451.00 28.21 DN

ATOM 8417CZ ARGD 129-19.00126.195-4.8121.00 28.79 DC

ATOM 8418NH1ARGD 129-19.20127.177-3.9431.00 27.14 DN

ATOM 8419NH2ARGD 129-20.03025.659-5.4691.00 28.32 DN

ATOM 8420C ARGD 129-13.71130.409-4.0611.00 27.46 DC

ATOM 84210 ARGD 129-14.11330.657-2.9271.00 25.22 DO

ATOM 8422N ASPD 130-12.52030.789-4.5121.00 29.07 DN

ATOM 8423CA ASPD 130-11.57231.538-3.6931.00 29.99 DC

ATOM 8424CB ASPD 130-12.11132.951-3.4361.00 31.68 DC

ATOM 8425CG ASPD 130-11.01834.007-3.4941.00 35.85 DC

ATOM 8426OD1ASPD 130-9.962 33.732-4.1071.00 37.68 DO

ATOM 8427OD2ASPD 130-11.20835.114-2.9451.00 38.62 D0 ATOM 8428C ASPD 130-11.24630.828-2.3671.00 28.09 DC

ATOM 84290 ASPD 130-11.04431.469-1.3351.00 27.75 DO

ATOM 8430N LEUD 131-11.18329.500-2.3981.00 28.03 DN

ATOM 8431CA LEUD 131-10.88528.755-1.1771.00 26.86 DC

ATOM 8432CB LEUD 131-11.23027.276-1.3441.00 25.91 DC

ATOM 8433CG LEUD 131-12.72426.933-1,4411.00 26.79 DC

ATOM 8434CD1LEUD 131-12.88425.456-1.7781.00 26.08 DC

ATOM 8435CD2LEUD 131-13.42427.267-0.1411.00 24.65 DC

ATOM 8436C LEUD 131-9.437 28.894-0.7251.00 27.44 DC

ATOM 8437O LEUD 131-9.178 28.9140.472 1.00 27.74 DO

ATOM 8438N LEUD 132-8.492 28.994-1.6601.00 28,63 DN

ATOM 8439CA LEUD 132-7.079 29.134-1.2741.00 30.60 DC

ATOM 8440CB LEUD 132-6.160 29.193-2.5031.00 28.13 DC

ATOM 8441CG LEUD 132-6.058 27.936-3.3751.00 29.49 DC

ATOM 8442CD1LEUD 132-7.157 27.954-4.4571.00 27.98 DC

ATOM 8443CD2LEUD 132-4.691 27.893-4.0491.00 27.25 DC

ATOM 8444C LEUD 132-6.850 30.382-0.4221.00 31.20 DC

ATOM 8445O LEUD 132-6.121 30.3470.569 1.00 31.22 DO

ATOM 8446N LYSD 133-7.479 31.485-0.8071.00 32.73 DN

ATOM 8447CA LYSD 133-7.325 32.736-0.0691.00 34.00 DC

ATOM 8448CB LYSD 133-7.824 33.909-0.9161.00 36.40 DC

ATOM 8449CG LYSD 133-7.953 35.230-0.1571.00 38.64 DC

ATOM 8450CD LYSD 133-8.254 36.371-1.1241.00 41.76 DC

ATOM 8451CE LYSD 133-8.423 37.718-0.4221.00 43.06 DC
ATOM 8452NZ LYSD 133-8.467 38.841-1.4241.00 43.80 DN

ATOM 8453C LYSD 133-8.087 32.6901.245 1.00 33.52 DC

ATOM 8454O LYSD 133-7.575 33.0942.283 1.00 35.01 DO
ATOM 8455N THRD 134-9.315 32.1921.206 1.00 33.10 DN

ATOM 8456CA THRD 134-10.12632.1172.415 1.00 30.82 0C
ATOM 8457CB THRD 134-11.53931.5742.094 1.00 30.72 DC
ATOM 8458OG1THRD 134-12.20132.4801.196 1.00 29.61 DO
ATOM 8459CG2THRD 134-12.36731.4073.387 1.00 28.09 DC
ATOM 8460C THRD 134-9.488 31.2443.489 1.00 30.17 DC
ATOM 8461O THRD 134-9.526 31.5814.665 1.00 29.54 D0 ATOM 8462N PHED 135-8.902 30.1183.098 1.00 30.63 DN

ATOM 8463CA PHED 135-8.286 29.239_4.0881.00 31.06 D C

ATOM 8464CB PHED 135-8.844 27.8283_.9421.00 30.49 D C

ATOM 8465CG PHED 135-10.29527.7354.280 1.00 32.06 D C

ATOM 8466CD1PHED 135-10.72427.8975.597 1.00 32.05 D C

ATOM 8467CD2PHED 135-11.24627.5403.283 1.00 31.24 D C

ATOM 8468CE1PHED 135-12.07227.8715.920 1.00 32.44 D C

ATOM 8469CE2PHED 135-12.60027.5143.597 1.00 31.76 D C

ATOM 8470CZ PHED 135-13.01627.6794.916 1.00 32.02 D C

ATOM 8471C PHED 135-6.760 29.2364.055 1.00 30.78 D C
ATOM 8472O PHED 135-6.119 28.3384.595 1.00 30.28 D 0 ATOM 8473N LYSD 136-6.199 30.2723.438 1.00 30.72 D N

ATOM 8474CA LYSD 136-4.758 30.4503.335 1.00 31.31 D C

ATOM 8475CB LYSD 136-4.194 31.0064.653 1.00 32.68 D C

ATOM 8476CG LYSD 136-4.853 32.3275.066 1.00 36.53 D C

ATOM 8477CD LYSD 136-4.209 32.9776.297 1.00 40.66 D C

ATOM 8478CE LYSD 136-5.125 34.0486.926 1.00 43.66 D C
ATOM 8479NZ LYSD 136-5.679 35.0385.932 1.00 44.97 D N

ATOM 8480C LYSD 136-4.051 29.1682.949 1.00 29.23 D C

ATOM 8481O LYSD 136-3,092 28.7543.577 1.00 29.57 D O
ATOM 8482N ILED 137-4.538 28.5391.894 1.00 28.79 D N
ATOM 8483CA ILED _137-3._933_27.309__1_4141.00 28.23 D C
ATOM 8484CB ILED 137-4.985 26.4180.718 1.00 26.77 D C

ATOM 8485CG2ILED 137-4.343 25.1660.194 1.00 24.84 D C

ATOM 8486CG1ILED 137-6.127 26.0911.679 1.00 28.49 D C

ATOM 8487CD1ILED 137-7.241 25.2601.028 1.00 26.90 D C

ATOM 8488C ILED 137-2.830 27.6320.394 1.00 27.01 D C
ATOM 8489O ILED 137-3.0$8 28.281-0.6081.00 27.01 D O

ATOM 8490N PROD 13_8_-1_.57_927.236__0_6691.00 27.73 D N
ATOM 8491CD PROD 138-0.95_9__26.965____1_.9_761.00 27.44 D C
ATOM 8492CA PROD 138-0.557 27.543-0.3391.00 28.12 D C

ATOM 8493CB PROD 1380.758 27.1450.346 1.00 27.78 D C

ATOM 8494CG PROD 1380.334 26.3671.581 1.00 28.31 D C

ATOM 8495C PROD 138-0.836 26.746-1.6181.00 28.95 D C

ATOM 8496O PROD 138-1.258 25.584-1.5631.00 27.91 D O

ATOM 8497N VALD 139-0.617 27.383-2.7661.00 30.06 D N

ATOM 8498CA VALD 139-0.878 26.745-4.0441.00 30.72 D C

ATOM 8499CB VALD 139-0.556 27.670-5.2451.00 31.91 D C

ATOM 8500CG1VALD 139-1.822 28.269-5.7831.00 31.72 D C

ATOM 8501CG2VALD 1390.415 28.760-4.8291.00 32.66 D C

ATOM 8502C VALD 139-0.107 25.463-4.2391.00 30.08 D C

ATOM 8503O VALD 139-0.681 24.447-4.6591.00 28.64 D O

ATOM 8504N ASPD 1401.192 25.511-3.9571.00 29.65 D N

ATOM 8505CA ASPD 1402.029 24.327-4.1301.00 30.15 D C

ATOM 8506CB ASPD 1403.502 24.664-3.8941.00 33.51 D C

ATOM 8507CG ASPD 1403.752 25.266-2.5251.00 39.08 D C

ATOM 8508OD1ASPD 1404.636 24.744-1.8071.00 42.29 D O

ATOM 8509OD2ASPD 1403.074 26.264-2.1641.00 42.03 D O

ATOM 8510C ASPD 1401.585 23.197-3.2031.00 28.45 D C

ATOM 8511O ASPD 1401.661 22.027-3.5681.00 27.14 D O

ATOM 8512N THRD 1411.097 23.537-2.0121.00 27.62 D N

ATOM 8513CA THRD 1410.639 22.492-1.1041.00 26.48 D C

ATOM 8514CB THRD 1410.404 23.0430.312 1.00 26.09 D C

ATOM 8515OG1THRD 1411.524 23.8450:701 1.00 25.44 D 0 ATOM 8516CG2THRD 1410.277 21.9061.303 1.00 24.42 D C

ATOM 8517C THRD 141-0.646 21.858-1.6661.00 26.04 D C

ATOM 8518O THRD 141-0.814 20.634-1.6231.00 25.24 D O

ATOM 8519N LEUD 142-1.522 22.681-2.2411.00 25.17 D N

ATOM 8520CA LEUD 142-2.774 22.180-2.8151.00 25.03 D C

ATOM 8521CB LEUD 142-3.668 23.338-3.2761.00 24.79 D C

ATOM 8522CG LEUD 142-4.998 22,919-3.9231.00 26.95 D C

ATOM 8523CD1LEUD .142-5.863 22.159-2.9101.00 24,43 D C

ATOM 8524CD2LEUD 142-5.738 24.164-4.4481.00 27.70 D C

ATOM 8525C LEUD 142-2.528 21.237-3.9891.00 24.26 D C

ATOM 8526O LEUD 142-3.094 20.139-4.0411.00 24.91 D O

ATOM 8527N ILED 143-1.697 21.668-4.9341.00 23.96 D N

ATOM 8528CA ILED 143-1.372 20.842-6.0901.00 23.21 D C

ATOM 8529CB ILED 143-0.500 21.607-7.1101.00 23.78 D C

ATOM 8530CG2ILED 143-0.024 20.655-8.2201.00 20.63 D C

ATOM 8531CG1ILED 143-1.325 22.746-7.7321.00 24.79 D C

ATOM 8532CDtILED 143-0.518 23.636-8.6741.00 27.37 D C

ATOM 8533C ILED 143-0.664 19.561-5.6551.00 23.66 D C

ATOM 8534O ILED 143-1.023 18.487-6.1011.00 25.49 D O

ATOM 8535N THRD 1440.323 19.669-4.7691.00 24.48 D N

ATOM 8536CA THRD 1441.033 18.479-4.2841.00 23.94 D C

ATOM 8537CB THRD 1442.097 18,866-3.2441.00 24.28 D C

ATOM 8538OG1THRD 144.3.024 19.779-3.8441.00 _ D O
24.82 ATOM 8539CG2THRD 1442.839 17.630-2.7551.00 21.94 D C

ATOM 8540C THRD 1440.045 17.481-3.6551.00 22 D C
.42 ATOM 8541O THRD 1440.063 16.281-3.9671.00 _ D O
__ 21.04 ATOM 8542N TYRD 145-0.814 17.976-2.7731.00 22.49 D N

ATOM 8543CA TYRD 145-1.814 17.119-2.1491.00 22.80 D C

ATOM 8544CB TYRD 145-2.704 17.895-1.1761.00 _ D C
23.63 ATOM 8545CG TYRD 145-3.808 17.019-0.5971.00 24.81 D C

ATOM 8546CD1TYRD 145-3.511 16.0100.336 1.00 25.13 D C

ATOM 8547CE1TYRD 145-4.492 15.1050.777 _ 23.99 D C
1.00 ATOM 8548CD2TYRD 145-5.119 17.117-1.0651.00 23.40 D C
I I I ~ ~ ~

ATOM8549CE2TYRD 1456.111 16.231-0.636 1.00 25.10 D C

ATOM5550CZ TYRD 145-5.788 15.2230.280 1.00 26.30 D C

ATOM8551OH TYRD 145-6.751 14.3270.659 1.00 23.46 D O

ATOM8552C TYRD 145-2.717 16.49 3 -3.2091.00 23.76 D C

ATOM8553O TYRD 145-2.910 15.282-3.218 1.00 21.56 D O

ATOM8554N LEUD 146-3.252 17.326-4.108 1.00 24.30 D N

ATOM8555CA LEUD 146-4.157 16.847-5.158 1.00 24.19 D C

ATOM8556CB LEUD 146-4.641 18.021-6.043 1.00 22.20 D C

ATOM8557CG LEUD 146-5.512 19.088-5.345 1.00 22.23 D C

ATOM8558CD1LEUD 146-6.033 20.108-6.374 1.00 20.59 D C
' ATOM8559CD2LEUD 146-6.682 18.415-4.623 1.00 20.08 D C

ATOM8560C LEUD 146-3.537 15.747-6.013 1.00 24.05 D C

ATOM8561O LEUD 146-4.182 14.729-6.288 1.00 22.44 D O

ATOM8562N METD 147-2.288 15.933-6.423 1.00 24.34 D N

ATOM8563CA METD 147-1.631 14.909-7.226 1.00 26.83 D C

ATOM8564CB METD 147-0.267 15.391-7.729 1.00 28.13 D C

ATOM8565CG METD 147-0.333 16.580-8.699 1.0D 31.31 D C

ATOM8566SD METD 1471.322 17.214-9.043 1.00 34.76 D S

ATOM8567CE METD 1471.028 18.287-10.4901.00 36.95 D C
' ATOM8568C METD 147-1.451 13.637-6.40.51.00 25.87 D C

ATOM8569O METD 147-1.593 12.530-6.927 1.00 26.66 D O
, ATOM8570N THRD 148-1.149 13.795-5.119 1.00 27.06 D N
' ATOM8571CA THRD 148-0.954 12.639-4.244 1.00 28.01 D C

ATOM8572CB THRD 148-0.475 13.047-2.853 1.00 29.22 D C

ATOM8573OG1THRD 1480.724 13.821-2.972 1.00 30.24 D O

ATOM8574CG2THRD 148-0.207 11.806-2.005 1.00 29.70 D C

ATOM8575C THRD 148-2.263 11.888-4.093 1.00 27.32 D C

ATOM8576O THRD 148-2.302 10.668-4.224 1.00 29.80 D O

ATOM8577N LEUD 149-3.334 12.622-3.830 1.00 25.66 D N

ATOM8578CA LEUD 149-4.638 12.012-3.683 1.00 26.60 D C

ATOM8579CB LEUD 149-5.696 13.073-3.388 1.00 24.77 D C

ATOM8580CG LEUD 149-7.125 12.521-3.393 1.00 24.86 D C

ATOM8581CD1LEUD 149-7.283 11.533-2.241 1.00 23.16 D C

ATOM8582CD2LEUD 149-8.138 13.665-3.268 1.0D 24.44 D C

ATOM8583C LEUD 149-5.013 11.272-4.965 1.00 27.00 D C

ATOM8584O LEUD 149-5.428 10.119-4.923 1.00 26.41 D O

ATOM8585N GLUD 150-4.872 11.947-6.103 1.00 27.50 D N

ATOM8586CA GLUD 1505.206 11.340-7.393 1.00 27.41 D C

ATOM8587CB GLUD 150-5.006 12.354-8.523 1.00 24.78 D C

ATOM8588CG GLUD 150-5.554 11.910-9.866 1.00 25.04 D C

ATOM8589CD GLUD 150-5.872 13.085-10.8001.00 26.18 D C

ATOM8590OE1GLUD 150-5.411 14.225-10.5201.00 23.75 D O

ATOM8591OE2GLUD 150-6.575 12.859-11.8171.00 23.64 D O

ATOM8592C GLUD 150-4.362 10.087-7.629 1.00 27.30 D C

ATOM8593O GLUD 150-4.878 9.067 -8.087 1.00 28.36 D O

ATOM8594N ASPD 151-3.073 10.171-7.303 1.00 28.13 D N

ATOM8595CA ASPD 151-2.146 9.037 -7.441 1.00 29.02 D C

ATOM8596CB ASPD 151-0.739 9.395 -6.905 1.00 29.95 D C

ATOM8597CG ASPD 1510.102 10.196-7.900 1.00 31.14 D C

ATOM8598OD1ASPD 1511.103 10.823-7.475 1.00 31.74 D O

ATOM8599OD2ASPD 151-0.220 10.189-9.105 1.00 31.45 D 0 ATOM8600C ASPD 151-2.649 7.829 -6.649 1.00 28.65 D C

ATOM86010 ASPD 151-2.319 6.693 -6.985 1.00 29.77 D 0 ATOM8602N HISD 152-3.427 8.063 -5.591 1.00 26.48 D N

ATOM8603CA HISD 152-3.901 6.941 -4.800 1.00 27.49 D C

ATOM8604CB H(SD 152-3.913 7.279 3.308 1.00 24.88 D C

ATOM8605CG HISD 152-2.550 7.254 -2.693 1.00 26.60 D C

ATOM8606CD2HISD 152-1.972 6.377 -1.838 1.00 26.52 D C

ATOM8607ND1HISD 152-1.582 8.191 -2.992 1.00 27.00 D N

ATOM8608CE1HISD 152-0.467 7.890 -2.351 1.00 25.20 D C

ATOM8609NE2HISD 152-0.676 6.795 -1.645 1.00 26.78 D N

ATOM8610C HISD 152-5.211 6.305 -5.223 1.00 27:28 D C

ATOM8611O HISD 152-5.709 5.405 -4.544 1.00 27.44 D O

ATOM8612N TYRD 153-5.771 6.775 -6.332 1.00 27,59 D N

ATOM8613CA TYRD 153-6.969 6.153 -6.888 1.00 27.72 D C

ATOM8614CB TYRD 153-7.843 7.143 -7.684 1.00 24,64 D C

ATOM8615CG TYRD 153-8.871 7.865 ~-6.85_01.00 20.60 D C

ATOM8616CD1TYRD 153-8.553 9.057 -6.189 _1.0_0_17.03 D C

ATOM8617CE1TYRD 153-9.464 9.672 -5.342 1.00 18.74 D C

ATOM8618CD2TYRD 153-10.1387.310 -6.648 1.00 19:56 D C

ATOM8619CE2TYRD 153-11.0667.918 -5.796 1.00 17.76 D C

ATOM8620CZ TYRD 153-10.7259.090 -5.143 1.00 20.18 D C

ATOM8621OH TYRD 153-11.6169.657 -4.254 1.00 20.52 D O

ATOM8622C TYRD 153-6.272 5.203 -7.848 1.00 29.82 D C

ATOM8623O TYRD 153-5.235 5.562 -8.421 1.00 30.39 D O

ATOM8624N HISD 154-6.815 4.004 -8.021 1.00 31.59 D N

ATOM8625CA HISD 154-6.191 3.016 -8.897 1.00 33.20 D C

ATOM8626CB HISD 154-6.600 1.599 -8.469 1.00 30.80 D G
ATOM8627CG HISD 154-6.247 1.274 -7.051 1.00 31.14 D C

ATOM8628CD2HISD 154-5.800 2.060 -6.041 1.00 30.66 D C

ATOM8629ND1HISD 154-6.379 0.007 -6.517 1.00 30.61 D N

ATOM8630CE1HISD 154-6.034 0.030 -5.243 1.00 29.88 D C

ATOM8631NE2HISD 154-5.678 1.263 -4.928 1.00 30.62 D N
ATOM8632C HISD 154-6.476 3.208 -10.3811.00 35.31 D C

ATOM8633O HISD 154-7.631 3.234 -10.8081.00 36.42 D O

ATOM8634N ALAD 155-5.411 3.321 -11.1671.00 36.07 D N

ATOM8635CA ALAD 155-5.536 3.488 -12.6091.00 38.76 D C
~

ATOM8636CB ALAD 155-4.192 3.929 _-13.2031.00 37.94 D C

ATOM8637C ALAD 155-6.029 2.228 _ -13.3361.00 39.73 D C
.--ATOM8638O ALAD 155-6.348 2.294 -14.5191.00 41.03 D 0 ATOM8639N ASPD 156-6.086 1.090 -12.6471.00 40.05 D N

ATOM8640CA ASPD 156-6.537 -0.152-13.2781.00 42.20 D C

ATOM8641CB ASPD 156-5.645 -1.325-12.8611.00 44.24 D C
.

ATOM8642CG ASPD 1565.669 -1.573-11.3641.00 46.55 D C

ATOM8643OD1ASPD 156-5.321 -0.647-10.5991.00 47.97 D O

ATOM8644002ASPD 156-6.029 -2.694-10.9471.00 48.77 D O

ATOM8645C ASPD 1b6-7.989 -0.490-12.9521.00 42.50 D C

ATOM8646O ASPD 156-8.506 -1.531-13.3631.00 41.33 D O

ATOM8647N VALD 157-8.636 0.391 -12.1981.00 42.82 D N

ATOM8648CA VALD 157-10.0290.207 -11.8221.00 42.19 D C

ATOM8649CB VALD 157-10.2680.683 -10.3791.00 43.02 D C

ATOM8650CGtVALD 157-11.7530,747 -10.0861.00 44.35 D C

ATOM8651CG2VALD 157-9.591 -0.279-9.407 1.00 42.81 D C

ATOM8652C VALD 157-10.8671.019 -12.8061.00 41.58 D C

ATOM8653O VALD 157-10.7452.245 -12.8771.00 41.35 D O

ATOM8654N ALAD 158-11.7130,319 -13.5591.00 39.30 D N

ATOM8655CA ALAD 158-12.5540,925 -14.5849.00 37.98 D C

ATOM8656CB ALAD 158-13.308-0.167-15.3321.00 _ D C
39.78 ATOM8657C ALAD 158-13.5332.004 -14.1481.0D 37.08 D C

ATOM8658O AlAD 158-13.8092._927-14.9201.00 36.33 D O

ATOM8659N TYRD 159-14.0561.907 -12.9301.00 35.60 D N

ATOM8660CA TYRD 959-15.0302.897 -12.4651.00 35.09 D C

ATOM8661CB TYRD 159-16.3442.195 -12.0851.00 34.87 D C

ATOM8662CG TYRD 159-17.4483.148 -11.701_ 34.46 D C
1.00 ATOM8663CD1TYRD 159-18.1573.847 -12.6791_.00 34.86 D C
ATOM8664CE1TYRD 159-19.1394.773 _-12.3331.00 34.15 D C

ATOM8665CD2TYRD 159-17.7513.394 -10.3611.00 34.08 D C

ATOM8666CE2TYRD 159-18.7294.320 -10.003_1.00 34.32 D C

ATOM8667CZ TYRD 159-19.4195.008 -11.0021.00 34.61 D C

ATOM8668OH TYRD 159-20.3815.937 -10,6751.00 34.40 D O

ATOM8669C TYRD 159-14.5743.770 -11.2891.00 34.23 D C
ATOM8670O TYRD 159-14.5144.995 -11.3961.00 31.95 D O

ATOM8671N HISD 160-14.2713,134 -10.1631.00 33.76 D N

ATOM8672CA HISD 160-13.8463.862 -8.974 1.00 33.46 D C

ATOM8673CB HISD 160-13.967_ -7.742 1.00 33.46 D C
2.972 ATOM8674CG HISD 160-15.3572,476 -7.498 1.00 36.32 D C

ATOM8675CD2HISD 160-16.3452.948 -6.699 1.00 34.78 D C

ATOM8676ND1HISD 160-15.8791.374 -8.143 1.00 36.55 D N

ATOM8677CE1HISD 160-17.f271.187 -7,750 1.00 37.17 D C

ATOM8678NE2HISD 160-17.4332.128 -6.874 1.00 35.73 D N

ATOM8679C HISD.160-12.4334.411 -9.073 1.00 31.27 D C

ATOM86800 HISD 160-11.5604.044 -8.298 1.00 31.85 D O

ATOM8681N ASND 161-12.2245.312 -10.0181.00 30.53 D N

ATOM8682CA ASND 161-10.9135.908 -10.2181.00 30.69 D C

ATOM8683CB ASND 161-10.4015.551 -11.6051.00 31.73 D C

ATOM8684CG ASND 161-i 1.3915.917 -12,6901.00 33.93 D C

ATOM8685OD1ASND 16t-11.9027.035 -1 1.00 32.25 D O
2.718 ATOM8686ND2ASND 161-11.6704.973 _ 1.00 34.81 D N
13.591 ATOM8687C ASND 161-10.9417.436 -10.0551.00 30.24 D C

ATOM8688O ASND 161-11.9468.027 -9.640 1.00 28.67 D 0 ATOM8689N ASND 162-9.825 8.065 -10.4001.00 29.56 D N

ATOM8690CA ASND 162-9.682 9.507 -10.2791.00 29.07 D C

ATOM8691CB ASND 162-8.266 9.914 -10.6571.00 29.24 D C

ATOM8692CG ASND 162-7.930 9.548 -12,0721.00 31.07 D C

ATOM8693OD7ASND 162-5.217 $.441 -12.5081.00 32.40 D O

ATOM8694ND2ASND 162-7.312 10.470-12.8041.00 31.97 D N

ATOM8695C ASND 162-10.67610.282-11,1351.00 27.97 D C

ATOM8696O ASND 162-10.94611.444-10.8501.00 27.54 D O

ATOM8697N ILED 163-11.2089.647 -12.1791.00 27.44 D N

ATOM8698CA ILED 163-12.16510.308-13.0601.00 26.74 D C

ATOM8699CB ILED 163-12.3019.587 -14.4311.00 27.31 D C

ATOM8700CG2ILED 163-13.180_10.433-15.3771.00 26.47 D C

ATOM8701CGtILED 163-10.9149.387 -15.0631.00 25.70 D C

ATOM8702CD1ILED 163' -10.9208.685 -16.4181.00 22.89 D C

ATOM8703C ILED 163-13.52610.366-12.3801.00 26.76 D C

ATOM8704O ILED 163-14.25211.355-12.5261.00 25.42 D O

ATOM8705N HISD 164-13.8559.310 -11.6281.00 27.01 D N

ATOM8706CA HISD 164-15.1119,231 -10.8811.00 24.77 D C

ATOM8707CB HISD 164-15.2937.815 -10.3031.00 25.35 D C

ATOM8708CG HISD 164-16.3757,707 -9.263 9.00 26.65 D C

ATOM8709CD2HISD 164-t6.3107,447 -T.933 1.00 27.01 D C

ATOM8710ND1HISD 164-17.7127.879 -9.552 1.00 26.30 D N

ATOM8711CE1HISD 164-18.4237,730 -8.447 1.00 27.55 D C

ATOM8712C HISD 164-14.98610.259-9.761 1.00 24.37 D C

ATOM8713O H1SD 164-15.89811.0459.497 1.00 23.94 D O

ATOM8714NE2HISD 164-17.5967,465 -7.448 1.00 28.17 D N

ATOM8715N ALAD 165-13.83010.262-9.112 1.00 24.27 D N

ATOM8716CA ALAD i65-13.58111.208-8.039 1.00 22.82 D C

ATOM8717CB ALAD 165-12.f6111.023-7.512 1.00 22.19 D C

ATOM8718C ALAD 165-13.77112.637-8.564 1.00 22.94 D C

ATOM8719O ALAD 165-14.41813.475-7.916 1.00 22.67 D O

ATOM8720N ALAD 166-13.21312.906-9.742 1.00 22.20 D N

ATOM 8721CA ALAD 166-13.30714.230-10.3541.00 23.06 D C

ATOM 8722CB ALAD 166-12.43914.300__ -11.6141.00 23.57 D C

ATOM 8723C ALAD 166-14.75214.550-10.6931.00 23.99 D C

ATOM 8724O ALAD 166-15.22015.663-10.4411.00 24.78 D O

ATOM 8725N ASPD 167-15.45913.572-11.2531.00 24.50 D N

ATOM 8726CA ASPD 167-16.86613.740-11.6121.00 25.84 D C

ATOM 8727CB ASPD 167-17.39112.441-12.2451.00 27.96 D C

ATOM 8728CG ASPD 167-18.79112.582-12.8341.00 29.69 D C

ATOM 8729OD1ASPD 167-19.10813.662-13.3961.00 28.98 D O

ATOM 8730OD2ASPD 167-19.56511.596-12.7591.00 29.82 D O

ATOM 8731C ASPD 167-17.70514.106-10.3741.00 25.87 D C

ATOM 8732O ASPD 167-18.43615.107-10.3741.00 26.49 D O

ATOM 8733N VALD 168-17.58513.305-9.317 1.00 24.30 D N

ATOM 8734CA VALD 168-18.33513.543-8.083 1.00 23.71 D C

ATOM 8735CB VALD 168-18.06912.421-7.041 1.00 23.69 D C

ATOM 8736CG1VALD 168-18.79412.703-5.755 1.00 21.31 D C

ATOM 8737CG2VALD 168-18.53711.089-7.605 1.00 23.06 D C

ATOM 8738C VALD 168-18.02014.911-7.471 1.00 23.87 D C

ATOM 8739O VALD 168-18.91415.571-6.919 1.00 23.78 D O

ATOM 8740N VALD 169-16.76215.342-7.569 1.00 22.59 D N

ATOM 8741CA VALD 169-16.38016.651-7.036 1.00 21.15 D C

ATOM 8742CB VALD 169-14.84516.904-7.151 1.00 22.01 D C

ATOM 8743CG1VALD 169-14.53718.406-7.003 1.00 18.26 D C

ATOM 8744CG2VALD 169-14.11316.108-6.082 1.00 21.45 D C

ATOM 8745C VALD 169-17.09317.749-7.822 1.00 21.18 D C

ATOM 8746O VALD 169-17.70518.653-7.255 1.00 20.44 D O

ATOM 8747N GLND t70-17.01317.652-9.140 1.00 21.87 D N

ATOM 8748CA GLND 170-17.62418.646-9,999 1.00 23.41 D C

ATOM 8749CB GLND 170-17.20318.418-11.4451.00 21.75 D C

ATOM 8750CG GLND 170-17.56519.546-12.3681.00 22.60 D C

ATOM 8751CD GLND 170-18.89319.314-13.0641.00 25.31 D C

ATOM 8752OE1GLND 170-19.27418.169-13.3231.00 23.56 D O

ATOM 8753NE2GLND 170-19.59220.398-13.3971.00 24.52 D N

ATOM 8754C GLND 170-19.13718.654-9.876 1.00 23.53 D C

ATOM 8755O GLN0 170-19.75619.706-9.981 1.00 25.08 D O
i ATOM 8756N SERD 171-19.73617.494-9.636 1.00 24.32 D N
' ATOM 8757CA SER1 171-21.19017.435-9.491 1.00 24.24 D C
D

ATOM 5758CB SER; 171-21.66915.983-9.555 1.00 24.25 D C
D

ATOM 8759OG SERD 171-21.31215.396-10.8051.00 27.43 D O

ATOM 8760C SERD 171-21.59418.078-8.160 1.00 24.59 D C

ATOM 8761O SERD 171-22.58618.815-8.069 1.00 25.73 D O

ATOM 8762N THRD 172-20.82217.805-7.121 1.00 23.36 D N

ATOM 8763CA THRD 172-21.12718.386-5.828 1.00 23.33 D C

ATOM 8764CB THRD 172-20.14217.875-4.756 1.00 21.95 D C

ATOM 8765OG1THRD 172-20.36916.480-4.549 1.00 21.42 D O

ATOM 8766CG2THRD 172-20.32618.615-3.451 1.00 19.69 D C

ATOM 8767C THRD 172-21.01619.900-5.948 1.00 22.91 D C

ATOM 8768O THRD 172-21.81120.643-5.377 1.00 23.45 D O

ATOM 8769N HISD 173-20.01220.343-6.695 1.00 22.37 D N

ATOM 8770CA HISD 173-19.77621.760-6.887 1.0D 23.65 D C

ATOM 8771CB HISD 173-18.5162_1.954-7.732 1.00 22.57 D C

ATOM 8772CG HISD 173-18.36823.337-8.281 1.00 24.34 D C

ATOM 8773CD2HISD 173-18.39423.795-9.554 1.00 23.79 D C

ATOM 8774ND1HISD 173-18.16724.441-7.481 1.00 25.29 D N

ATOM 8775CE1HISD 173-18.071_25.520-8.238 1.00 23.36 D C

ATOM 8776NE2HISD 173-18.20425.154-9.501 1.00 23.69 D N

ATOM 8777C HISD 173-20.98422.439-7.564 1.00 23.82 D C

ATOM 8778O HISD 173-21.34123.572-7.244 1.00 22.44 D O

ATOM 8779N VALD 174-21.59421.744-8.514 1.00 23.42 D N

ATOM 8780CA VALD 174-22.74722.300-9.193 1.00 24.37 D C

ATOM 8781CB VALD 174-23.10321.466-10.4481.00 25.27 D C

ATOM 8782CG1VALD 174-24.41921.964-11.0651.00 24.32 D C

ATOM 8783CG2VALD 174-21.97321.582-11.4621.00 23.02 D C

ATOM 8784C VALD 174-23.91022.348-8.220 1.0D 23.33 D C

ATOM 8785O VALD 174-24.56223.380-8.080 1.00 25.23 D O

ATOM 8786N LEUD 175-24.14721.240-7.532 1.0_0 23.65 D N

ATOM 8787CA LEUD 175-25.22521.158-6.550 1.00 25.14 D C

ATOM 8788CB LEUD 175-25.26219.765-5.921 1.00 25.01 D C

ATOM 8789CG LEUD 175-25.54918.636-6.905 1.00 25.63 D C

ATOM 8790CD1LEUD 175-25.57017.314-6.164 1.00 25.31 D C

ATOM 8791CD2LEUD 175-26.87818.882-7.600 1.00 24.47 D C

ATOM 8792C LEUD 175-25.12522.216-5.447 1.00 25.63 D C

ATOM 8793O LEUD 175-26.14122.738-5.005 1.00 25.91 D O

ATOM 8794N LEUD 176-23.90822.519-4.996 1.00 26.18 D N

ATOM 8795CA LEUD 176-23.70723.540-3.972 1.00 26.34 D C

ATOM 8796CB LEUD 176-22.23223.596-3.541 1.00 25.31 D C

ATOM 8797CG LEUD 176-21.63822.556-2.592 1.00 26.15 D C

ATOM 8798CD1LEUD 176-20.12322.718-2.533 1.00 26.00 D C

ATOM 8799CD2LEUD 176-22.24622.719-1.207 1.00 24.84 D C

ATOM 8800C LEUD 176-24.11224.924-4.501 1.00 27.06 D C

ATOM 88010 LEUD 176-24.49925.790-3.728 1.00 29.12 D O

ATOM 8802N SERD 177-24.02325.124-5.813 1.00 26.56 D N

ATOM 8803CA SERD 177-24.34826.423-6.424 1.00 28.60 D C

ATOM 8804CB SERD 177-23.53226.642-7.709 1.00 26.70 D C

ATOM 8805OG SERD 177-22.19126.242-7.553 1.00 30.44 D O

ATOM 8806C SERD 177-25.81726.612-6.791 1.00 27.90 D C

ATOM8807O SER D 177-26.17627.646-7.335 1.00 26.65 D O

ATOM8808N THR D 178-26.64525.606-6.521 1.00 28.60 D N

ATOM8809CA THR D 178-28.06425.668-6.848 1.00 29.47 D C
~

ATOM8810CB THR D 178-28.78824.354-6.401 1.00 31.18 D C

ATOM8811OG1THR D 178-29.88724.097-7.272 1.00 31.74 D O

ATOM8812CG2THR D 178-29.31524.462-4.978 1.00 32.04 D C

ATOM8813C THR D 178-28.68226.895-6.176 1.00 27.87 D C

ATOM8814O THR D 178-28.34927.212-5.046 1.00 26.38 D O

ATOM8815N PRO D 179-29.57427.615-6.884 1.00 28.22 D N

ATOM8816CD PRO D 179-29.97327.400-8.290 1.00 27.61 D C

ATOM8817CA PRO D 17930.221 28.816-6.328 1.00 27.83 D C

ATOM8818CB PRO D 179X1.284 29.153-7.373 1.00 26.82 D C
~

ATOM8819CG PRO D 179-30,61828.739-8.657 1.00 27.62 D C

ATOM8820C PRO D 179-30.82328.606-4.940 1.00 28.10 D C
, ATOM8821O PRO D 179-30.57729.393-4.028 1.00 28.16 D O

ATOM8822N ALA D 180-31.59327.532-4.786 1.0D 27.42 D N

ATOM8823CA ALA D 180-32.24527.228-3.518 1.00 29.05 D C

ATOM8824CB ALA D 180-33.08525.981-3.660 1.00 28.02 D C

ATOM8825C ALA D 180-31.29327.081-2.324 1.00 29.53 D C

ATOM8826O ALA D 180-31.73927.088-1.173 1.00 29.59 D O

ATOM8827N LEU D 181-29.99226.963-2.579 1.00 29.27 D N

ATOM8828CA LEU D 181-29.04026.832-1.477 1.00 30.10 D C

ATOM8829CB LEU D 181-28.23725.550-1.623 1.00 29.81 D C

ATOM8830CG LEU D 181-29.11824.307-1.620 1.00 31.34 D C

ATOM8831CD1LEU D 181-28.29023.095-1.983 1.00 30.85 D C

ATOM8832CD2LEU D 181-29.75324.146-0.241 1.00 32.84 D C

ATOM8833C LEU D 181-28.08728.006-1.379 1.00 31.05 D C

ATOM8834O LEU D 181-27.08127.934-0.670 1.00 32.37 D O

ATOM8835N GLU D 182-28.40329.094-2.067 1.00 30.77 D N

ATOM8836CA GLU D 182-27.51830.251-2.045 1.00 32.98 D C

ATOM8837CB GLU D 182-28.02431.329_-3.011 1.00 32.06 D C

ATOM8838CG GLU D 182-27.03932.468-3.197 1.00 34.09 D C

ATOM8839CD GLU D 182-27.49433_.507-4.218 1.00 35.97 D C

ATOM8840OE1GLU D 182-26.83634.577-4.306 1.00 37.67 D O

ATOM8841OE2GLU D 182-28.49133.255-4.935 1.00 33.42 D O

ATOM8842C GLU D 182-27.31530.841-0.641 1.00 33.69 D C

ATOM8843O GLU D 182-28.27731.1130.093 1.00 33.62 D O

ATOM8844N ALA D 183-26.04631.010-0.276 1.00 33.17 D N

ATOM8845CA ALA D 183-25.65031.5571.023 1.00 32.50 D C

ATOM8846CB ALA D 183-26.14833.0031.155 1.00 32.52 D C

ATOM8847C ALA D 183-26.10030.7232.234 1.00 32.26 D C

ATOM88480 ALA D 183-26.01231.1803.378 1.00 33.97 D O

ATOM5849N VAL D 184-26.57329.5041.985 1.00 31.60 D N

ATOM8850CA VAL D 184-27.01128.6183.061 1.00 31.06 D C

ATOM8851CB VAL D 184-27.88927.466_2.521 1.00 31.12 D C

ATOM8852CG1VAL D 184-28.20326.4853.638 1.00 30.55 D C

ATOM8853CG2VAL D 184-29.19028.0191.918 1.00 30.92 D C

ATOM8854C VAL D 184-25.82227.9833.800 1.00 31,61 D C

ATOM8855O VAL D 184-25.83927.8505.023 1.00 33.60 D O

ATOM8856N PHE D 185-24.79827.5803.055 1.00 30.46 D N

ATOM8857CA PHE D 185-23.62826.9423.643 1.00 29.05 D C

ATOM8858CB PHE D 185-23.23325.7212.810 1.00 29.36 D C

ATOM8859CG PHE D 185-24.21424.5882.898 1.00 28.04 D C

ATOM8860CD1PHE D 185-24.41023.9104.104 1.00 29.06 D C

ATOM8861CD2PHE D 185-24.95924.2071.787 1.00 27.88 D C

ATOM8862CE1PHE D 185-25.33722.8654.205 1.00 27.87 D C

ATOM8863CE2PHE D 185-25.88923.1671.874 1.00 27.64 D C

ATOM8864CZ PHE D 185-26.08022.4953.087 1.00 27.80 D C

ATOM8865C PHE D 185-22.42127.8593.800 1.00 28.90 D C

ATOM8866O PHE D 185-22.14728.7112.958 1.00 29.01 D O

ATOM8867N THR D 186-21.70027.6854.898 1.00 28.23 D N

ATOM8868CA THR D 186-20.51028.4875.145 1.00 27.02 D C

ATOM8869CB THR D 186-20.03128.3556.602 1.00 26.57 D C

ATOM8870OG1THR D 186-19.65626.9946.845 1.00 26.21 D O

ATOM8871CG2THR D 186-21.14728.7597.588 1.00 25.04 D C

ATOM8872C THR D 186-19.41227.9494.240 1.00 26.76 D C

ATOM8873O THR D 186-19.55726.8973.612 1.00 25.87 D O

ATOM8874N ASP D 187-18.30828.6744.182 1.00 28.98 D N

ATOM8875CA ASP D 187-17.18328.2683.370 1.00 29.86 D C

ATOM8876CB ASP D 187-16.15829.3893.322 1.00 34.04 D C
' ATOM8877CG ASP D 187-16.64230.5702.500 1.00 37.28 D C

ATOM8878OD1ASP D 187-16.79530.4281.259 1.00 39.30 D O

ATOM8879OD2ASP D 187-16.87831.6343.100 1.00 41.08 D O

ATOM8880C ASP D 187-16.55126.9983.902 1.00 29.58 D C

ATOM88810 ASP D 187-16.05426.1803.120 1.00 29.91 D O

ATOM8882N LEU D 188-16.58926.8205.222 1.00 29.11 D N

ATOM8883CA LEU D 188-16.00225.6325.834 1.00 29.55 D C

ATOM8884CB LEU D 188-15.89525.7787.353 1.00 29.27 D C

ATOM8885CG LEU D 188-15.06824.6968.066 1.00 29.56 D C

ATOM8886CD1LEU D 188-13.63124.7387.572 1.00 27.88 D C

ATOM8887CD2LEU D 188-15.09724.9279.582 1.00 29.76 D C

ATOM8888C LEU D 188-16.84124.4145.504 1.00 29.26 D C

ATOM8889O LEU D 188-16.31923.3095.371 1.00 29.11 D 0 ATOM8890N GLU D 189-18.14724.6135.369 1.00 28.57 D N

ATOM8891CA GLU D 189-19.02523.5085.026 1.00 28.57 D C

ATOM8892CB GLU D 189-20.47523.8815.375 1.00 30.16 D C

ATOM8893CG GLUD 189-20.69324.0666.889 1.00 33.19 D C

ATOM8894CD GLUD 189-21.97124.8217.244 1.00 34.90 D C

ATOM8895OE1GLUD 189-22.17825.9416.738 1.00 38.59 D O

ATOM8896OE2GLUD 189-22.77424.3078.041 1.00 37.51 D 0 ATOM8897C GLUD 189-18.85823.1793.536 1.00 27.39 D C

ATOM8898O GLUD 189-18.90322.0143.128 1.00 28.34 D 0 ATOM8899N ILED 190-18.64724.2122.728 1.00 27.12 D N

ATOM8900CA ILED 190-18.45624.0461.288 1.00 25.96 D C

ATOM8901CB ILED 190-18.40125.4310.572 1.00 24.44 D C

ATOM8902CG2ILED 190-17.86425.281-D.822 1.00 21.98 D C

ATOM8903CGtILED 190-19.79126.0690.568 1.00 25.29 D C

ATOM8904CD1ILED 190-19.85427.5010.021 1.00 21.07 D C

ATOM8905C ILED 190-17.14623.2941.055 1.00 25.09 D C

ATOM8906O ILED 190-17.08122.3720.238 1.00 25.56 D O

ATOM8907N LEUD 191-16.11023.7001.786 1.00 24.68 D N

ATOM8908CA LEUD 195-14.78723.0831.690 1.00 24.48 D C

ATOM8909CB LEUD 191-13.80223.8032.631 1.00 24.74 D C

ATOM8910CG LEUD 191-12.44123.1342.868 1.00 24.30 D C

ATOM8911CD1LEUD 191-11.73122.9171.532 1.00 24.75 D C

ATOM8912CD2LEUD 191-11.59023.9933.799 1.00 24.00 D C

ATOM8913C LEUD 191-14.87821.6142.071 1.00 23.36 D C

ATOM8914O LEUD 191-14.28420.7471.432 1.00 24.44 D O

ATOM8915N ALAD 192-15.63221.3443.128 1.00 23.54 D N

ATOM8916CA ALAD 192-15.82919.9843.601 1.00 23.12 D C

ATOM8917CB ALAD 192-16.65720.0074.868 1.00 24.98 D C
' ATOM8918C ALAD 192-16.51719.1102.556 1.00 23.84 D C
~

ATOM8919O ALAD 192-16.07717.9862.287 1.00 23.10 D O
' ATOM8920N ALAD 193-17.59819.6241.961 1.00 22.36 D N

ATOM8921CA ALAD 193-18.34318.8440.978 1.0D 22.30 D C

ATOM8922CB ALAD 193-19.61519.5830.579 1.00 21.82 D C
' ATOM8923C ALAD 193-17.49718.538-0.252 1.00 22.74 D C

ATOM8924O ALAD 193-17.56217.440-0.810 1.00 19.71 D O

ATOM8925N ILED 194-16.70219.520-0.674 1.00 23.52 D N

ATOM8926CA ILED 194-15.85219.329-1.838 1.00 24.20 D C

ATOM8927CB ILED 194-15.25420.667-2.356 1.00 26.13 D C

ATOM8928CG2ILED 194-14.25620.388-3.519 1.00 22.07 D C

ATOM8929CG1ILED 194-16.37921.586-2.820 1.00 26.59 D C

ATOM8930CD1ILED 194-15.91422.958-3.234 1.00 29.47 D C

ATOM8931C ILED 194-14.70818.394-1.487 1.00 23.16 D C

ATOM8932O ILED 194-14.42717.458-2.234 1.00 22.02 D O

ATOM8933N PHED 195-14.05018.644-0.357 1.00 22.63 D N

ATOM8934CA PHED 195-12.93617.7750.041 1.00 24.69 D C

ATOM8935CB PHED 195-12.29718.2361.354 1.00 24.76 D C

ATOM8936CG PHED 195-11.15117.3651.793 1.00 28.05 D C

ATOM8937CD1PHED 195-9.943 17.3801.103 1.00 27.49 D C

ATOM8938CD2PHED 195-11.29516.4912.865 1.00 27.44 D C

ATOM8939CE1PHED 195-8.885 16.5291.472 1.00 28.24 D C

ATOM8940CE2PHED 195-10.25515.6433.240 1.00 29.62 D C

ATOM8941CZ PHED 195-9.040 15.6612.536 1.00 29.27 D C

ATOM8942C PHED 195-13.44716.3410.199 1.00 23.66 D C

ATOM8943O PHED 195-12.83415.402-0.306 1.00 24.30 D O

ATOM8944N ALAD 196-14.58316.1760.873 1.00 23.05 D N

ATOM8945CA ALAD 196-15.16214.8441.057 1.00 23.11 D C

ATOM8946CB ALAD 196-16.50214.9351.808 1.0D 24.34 D C

ATOM8947C ALAD 196-15.37714.179-0.291 1.00 22.73 D C

ATOM89480 ALAD 196-15.10012.988-0.458 1.00 23.77 D O

ATOM8949N SERD 197-15.86114.945-1.264 1.00 21,12 D N

ATOM8950CA SERD 197-16.09914.369-2.572 1.00 21.84 D C

ATOM8951CB SERD 197-16.81415.369-3.491 1.00 22.58 D C

ATOM8952OG SERD 197-18.11315.651-3.020 1.00 23.52 D O

ATOM8953C SERD 197-14.82613.884-3.248 1.00 21.75 D C

ATOM8954O SERD 197-14.84112.848-3.902 1.00 20.59 D O

ATOM8955N ALAD 198-13.73114.627-_3.0921.00 22.32 D N

ATOM8956CA ALAD 198-12.45514.2623.719 1.00 22.88 D C

ATOM8957CB ALAD 198-11.44415.427-3.580 1.00 21.57 D C

ATOM8958C ALAD 198-11.84212.977-3.154 1.00 23.35 D C

ATOM89590 ALAD 198-11.16512.238-3.570 1.00 24.42 D O

ATOM8960N ILED 199-12.07112.705-1.875 1.00 24.25 D N

ATOM8961CA ILED 199-11.49111.509-1.264 1.00 25.36 D C

ATOM8962CB ILED 199-10.89211.8050.136 1.00 25.35 D C

ATOM8963CG2ILED 199-10,04313.0700.096 1.00 24.50 D C

ATOM8964CG1ILED 199-12.00911.9741.166 1.00 26.10 D C

ATOM8965CD1ILED 199-11.50112.0732.618 1.00 25.09 D C

ATOM8966C ILED 199-12.44610.347-1.077 1.00 25.51 D C

ATOM8967O ILED 199-12.0149.250 -0.712 1.00 25.92 D O

ATOM8968N HISD 200-13.72710.561-1.365 1.0D ~ 24.92D N

ATOM8969CA HISD 200-14.7219.533 -1.108 1.00 23.66 D C

ATOM8970CB HISD 200-16.08810.010-1.566 1.00 24.65 D C

ATOM8971CG HiSD 200-16.4759.517 -2.918 1.00 24.39 D C

ATOM8972CD2HISD 200-17.2178.450 -3.293 1.00 25.72 D C

ATOM8973ND1HISD 200-16.05310.121-4.080 1.00 26.61 D N

ATOM8974CE1HISD 200-16.5169.444 -5.116 1.00 27.92 D C

ATOM8975C HISD 200-14.4888.102 -1.588 1.00 25.25 D C

ATOM8976O HISD 200-15.0777.176 -1.045 1.00 27.06 D O

ATOM8977NE2HISD 200-17.2258.426 -4.663 1.00 30.20 D N

ATOM8978N ASPD 201-13.6727.888 -2.604 1.00 25.40 D N

ATOM8979CA ASPD 201-13.4336.514 -3.042 1.00 27.60 D C

ATOM8980CB ASPD 201-14.1626.204 -4.370 1.00 32.74 D C

ATOM8981CG ASPD 201-15.6385.816 -4.173 1.00 35.72 D C

ATOM8982C ASPD 201-11.9476.278 -3.226 1.00 25.36 D C

ATOM$983O ASPD 201-11.5415.379 3.957 1.00 22.50 D O

ATOM8984OD1ASPD 201-15.9645.255 -3.103 1.00 44.00 D O

ATOM8985OD2ASPD 201-16.4686.062 -5.090 1.00 36.42 D 0 ATOM8986N VALD 202-11.1247.072 -2.554 1.00 25.42 D N

ATOM8987CA VALD 202-9.694 6.917 -2.765 1.00 27.57 D C

ATOM8988CB VALD 202-8.862 8.039 -2.055 1.00 27.58 D C

ATOM8989CG1VALD 202-8.927 7.898 -0.542 1.00 24.59 D C

ATOM8990CG2VALD 202-7.412 7.995 -2.566 1.00 27.68 D C

ATOM8991C VALD 202-9.213 5.533 -2.357 1.00 27.30 D C

ATOM8992O VALD 202-9.705 4.958 -1.395 1.00 26.67 D O

ATOM8993N ASPD 203-8.280 5.001 -3.139 1.00 28.06 D N

ATOM8994CA ASPD 203-7.696 3.681 -2.924 1.00 30.82 D C

ATOM8995CB ASPD 203-6.912 3.658 -1.600 1.00 29.77 D C

ATOM8996CG ASPD 203-5.989 2.453 -1.493 1.00 31.90 D C

ATOM8997OD1ASPD 203-5.525 1.967 -2.550 1.00 32.79 D O

ATOM8998OD2ASPD 203-5.717 1.996 -0.356 1.00 33.06 D O
ATOM8999C ASPD 203-8.720 2.530 -2.970 1.00 32.81 D C

ATOM9000O ASP0 203-8.596 1.536 -2.243 1.00 32.49 D O

ATOM9001N HISD 204-9.727 2.673 3.829 1.00 33.98 D N

ATOM9002CA HISD 204-10.7531.646 -4.003 1.00 35.32 D C

ATOM9003CB HISD 204-11.8962.195 -4.855 1.00 33.98 D C

ATOM9004CG HISD 204-13.1971.476 ~t.669 1.00 34.32 D C
ATOM9005CD2HISD 20414.357 1.872 -4.092 1.00 34.$0 D C

ATOM9006ND1HISD 204-13.4140.192 5.121 1.00 34.55 D N

ATOM9007CE7HISD 204-14.649-0.173-4.832 1.00 34.33 D C

ATOM900$NE2HISD 204-15.2440.828 -4.20$ 1.00 37.18 D N
ATOM9009C HISD 204-10.0970.459 -4.719 1.00 36.56 D C
ATOM9010O HISD 204-9.484 0.617 -5.770 1.00 38.23 D O
ATOM9011N PROD 205-10.214-0.746-4.153 1.00 37.68 D N

ATOM9012CD PROD 205-10.919-1.060-2.896 1.00 37.65 D C

ATOM9013CA PROD 205-9.621 -1.955-4.750 1.00 38.23 D C

ATOM9014CB PROD 205-9.728 -2.970-3.624 1.00 37.90 D C
ATOM9015CG PROD 205-11.040-2.568-2.962 1.00 38.93 D C

ATOM9016C PROD 205-10.313-2.452-6.028 1.00 39.00 D C
ATOM9017O PROD 205-9.722 -3.193-6.819 1.00 39.47 D O

ATOM9018N GLYD 206-11.566-2.048-6.220 1.00 38.54 D N

ATOM9019CA GLYD 206-12.309-2.483-7.385 1.00 3 D C

.91 ATOM__ C _ D 206_ -3.568-7.046 1.00 _ D C
ATOM9020O GLYD. 206-13.317-4.153-7.942 1.00 _ D O
ATOM9021N GLYD 207-13.922-3.840-5.753 1.00 40.56 D N
9022 VAL -13.487 41.73 41.89 ATOM9023CA VALD 207-14.433-4.848-5.265 1.00 42.98 D C

ATOM9024CB VALD 207-13.716-F.123-4.764 1.00 41.85 D C

ATOM9025CG1VALD 207-13.000-6.814-5.916 1.00 42.04 D C

ATOM9026CG2VALD 207-12.751-5.768-3.665 1.00 39.70 D C
ATOM9027C VALD 207-15.270-4.305-4.107 1.00 44.11 D C
ATOM90280 VALD 207-14.833-3.428-3.365 1.00 44.22 D O

ATOM9029N SERD 208-16.46811.851-3.94$ 1.00 45.90 D N

ATOM9030CA SERD 208-17.3854.419 -2.899 1.00 47.34 D C

ATOM9031CB SERD 208-18.774-4.999-3.177 1.00 48.35 D C

ATOM9032OG SERD 208-18.714-6.409-3.344 1.00 49.68 D O

ATOM9033C SERD 208-16.948-4.795-1.487 1.00 47.71 D C

ATOM9034O SERD 208-16.024-5.581-1.296 1.00 47.16 D 0 ATOM9035N ASND 209-17.619-4.219-0.497 1.00 49.37 D N

ATOMX36 CA ASND 209-17.317x.514 0.900 1.0D 51.42 D C

ATOM9037CB ASND 209-18.2003.683 1.833 1.00 50.65 D C

ATOM9038CG ASND 209-17.774-2.2401.907 1.0D 50.45 D C

ATOM9039OD1ASND 209-16.619-1.9432.201 1.00 50.89 D 0 ATOM9040ND2ASND 209-18.707-1.3321.655 1.00 50.43 D N

ATOM9041C ASND 209-17.572-5.9931.170 1.00 52.35 D C

ATOM9042O ASND 209-96.785-6.6511.851 1.00 53.11 D O

ATOM9043N GLND 210-18.679-6.4990.628 1.00 53.11 D N

ATOM9044CA GLND 210-19.064-7.8970.796 1.00 54.14 0 C

ATOM9045CB GLND 210-20.275-8.232-0.086 1.00 55.42 p C

ATOM9046CG GLND 210-20.951-9.5380.298 1.00 57.01 D C

ATOM9047CD GLND 210-21.553-9.4771.692 1.00 57.90 D C

ATOM9048OE1GLND 210-22.675-8.9991.874 1.00 59.24 D O

ATOM9049NE2GLND 210-20.800-9.9402.688 1.00 57.15 D N

ATOM9050C GLND 210-17.90$-8.8180.433 1.00 53.87 D C

ATOM9051O GLND 210-17.581-9.7371,180 1.00 53.53 D O

ATOM9052N PHED 211-17.292-8.565-0.719 1.00 53.95 D N

ATOM9053CA PHED 211-16.164-9.370-1.174 1.D0 54.02 D C

ATOM9054CB PHED 211-15.725-8.906-2.563 1.00 53.92 D C

ATOM9055CG PHED 211-14.526-9.6333.104 1.00 54.55 D C

ATOM9056CD1PHED 211-13.263-9.431-2.559 1.00 54.50 0 C

ATOM9057CD2PHED 211-14.655-10.503-4.182 1.00 55.64 D C

ATOM9058CEtPHED 211-12.146-10.082-3.079 1.00 54.82 D C

ATOM9059CE2PHED 211-13.541-11.162-4.712 1.00 55.55 D C

ATOM9060CZ PHED 211-12.285-10.947-4.157 1.00 54.83 D C

ATOM9061C PHED 211-15.001-9.273-0.192 1.00 54.35 D C

ATOM9062O PHED 211-14.351-10.2760.098 1,0D 55.17 D 0 ATOM9063N LEUD 212-14.741-8.0690.318 1.00 54.23 D N

[ 9064CA LEUD 212-13.648-7.8571.266 1.00 54 ATOM( I I I I I I ~ ~ 20 I

ATOM 9065CB LEUD 212-13.418-6.3601.505 1.00 53.58 D C

ATOM 9066CG LEUD 212-12,8995.506 _ 0,3411.00 53.80 D C

ATOM 9067CDtLEUD 212-12.758-4.059_ 0.7921.00 53.30 D C

ATOM 9068CD2LEUD 212-11.559-6.036-0.138 1.00 53.17 D C

ATOM 9069C LEUD 212-13.942-8.5392.593 1.00 54.88 D C

ATOM 9070O LEUD 212-13.031-8.9533.307 1.0D 54.59 D O

ATOM 9071N ILED 213-15.224-8.6362.924 1.00 55.46 D N

ATOM 9072CA ILED 213-15.658-9.2744.159 1.00 56.35 D C

ATOM 9073CB ILED 213-17.113-8.8724.506 1.0D 56.87 D C

ATOM 9074CG2ILED 213-17.630-9.7065.682 1.00 57.13 D C

ATOM 9075CG1ILED 213-17.177-7.3774.830 1.00 56.94 D C

ATOM 9076CD1ILED 213-18.591-6.8334.913 1.00 55.94 D C

ATOM 9077C ILED 213-15.594-10.7984.028 1.00 56,55 D C

ATOM 9078O ILED 213-15.135-11,4894.938 1.00 56,43 D O

ATOM 9079N ASND 214-16.043-11.3142.888 1.00 56.70 D N

ATOM 9080CA ASND 214-16.056-12.7552.656 1.00 57.53 D C

ATOM 9081CB ASND 214-17.049-13.1091.543 1.00 58.42 D C

ATOM 9082CG ASND 214-18.479-12.7371.891 1.00 59.39 D C

ATOM 9083OD1ASND 214-18.786-12.3893.035 1,00 58.76 D O

ATOM 9084ND2ASND 214-19.368-12.8180.900 1.00 59.58 D N

ATOM 9085C ASND 214-14.703-13.3822.321 1.00 57.73 D C

ATOM 9086O ASND 214-14.660-14.4961.794 1.00 57.47 D O

ATOM 9087N THRD 215-13.609-12.6742.601 1.00 57.16 D N
I

ATOM 9088CA THRD 215-12.274-13.2162.347 1.00 56.97 D C
' ATOM 9089CB THRD 215-11.578-12.5531.127 1.00 57.30 D C

ATOM 9090OG1THRD 215-11.341-11.1671.395 1.00 58.63 D O

ATOM 9091CG2THRD 215-12,433-12.691-0.126 1.00 57.90 D C

ATOM 9092C THRD 215-11.412-12.9873.577 1.00 57.07 D C

ATOM 9093O THRD 215-10.257-13.4113.630 1.00 56.63 D O
.

ATOM 9094N ASND 216-11,996-12.3294.575 1.00 57.50 D N

ATOM 9095CA ASND 216-11.292-12.017 5.8171.00 58,64 D C
~

ATOM 9096CB ASND 216-10.860-13.3026.542 1.00 59.85 D C

ATOM 9097CG ASND 216-12.021-14,0047.221 1.00 61.11 D C

ATOM 9098OD1ASND 216-12.505-13.5648.270 1.00 61.58 D O

ATOM 9099ND2ASND 216-12.491-15.0926.615 1.0D 62.84 D N

ATOM 9100C ASND 216-10.079-11.1445.525 1.00 58.07 D C

ATOM 9101O ASND 216-9.033 -11.2776.162 1.04 58.08 D O

ATOM 9102N SERD 217-10.237-10.2474.557 1.00 57,47 D N

ATOM 9103CA SERD 217-9.174 -9.3354.172 1.00 57.00 D C

ATOM 9104CB SERD 217-9.622 -8.4652.994 1.00 57.89 D C

ATOM 9105OG SERD 217-10.793-7.7383.315 1.00 59.31 D O

ATOM 9106C SERD 217-8.808 -8.4585.353 1.00 56.10 D C

ATOM 9107O SERD 217-9.665 -8.0976.161 1.00 56.38 O O

ATOM 9108N GLUD 218-7.527 -8.1285.454 1.00 55.69 D N

ATOM 9109CA GLUD 218-7.031 -7.2846.536 1.00 55.30 D C

ATOM 9110CB GLUD 218-5.564 -6.9246.265 1.00 55.05 D C

ATOM 9111CG GLUD 218-5.000 -5.8067.124 1.00 55.67 D C

ATOM 9112CD GLUD 218-3.539 -5.5086.804 1.00 57.08 D C

ATOM 9113OE1GLUD 2183.139 5.626 5.622 1.00 57,30 D O

ATOM 9114OE2GLUD 218-2.789 5.142 7.734 1.00 57.62 D O

ATOM 9115C GLUD 218-7,882 -6.0166.691 1.00 54.52 D C

ATOM 9116O GLUD 218-8.056 -5.5067.796 1.00 54.96 D O

ATOM 9117N LEUD 219-8.420 -5.5255.578 1.00 53 .13D N

ATOM 9118CA LEUD 219-9.248 -4.3215.578 1.00 51 .96D C

ATOM 9119CB LEUD 219x.510 3.887 4,130 1.00 51 .76D C

ATOM 9120CG LEUD 219-9.849 -2.4153.843 1.00 51.27 D C

ATOM 9127CD1LEUD 219-8.828 -1.4974.497 1.00 50.27 D C

ATOM 9122CD2LEUD 219-9.867 -2.1992.338 1.00 50.97 D C

ATOM 9123C LEUD 219-10.567-4.5666.304 1.00 50.88 D C

ATOM 9124O LEUD 219-10.929-3.8747.244 1.00 49.39 D O

ATOM 9125N ALAD 220-11.2735.623 5.862 1.00 50.76 D N

ATOM 9126CA ALAD 220-12.546-6.0096.460 1.00 50.73 D C

ATOM 9127CB ALAD 220-13.141-7.2025.703 1.00 50.58 D C

ATOM 9128C ALAD 220-12.393-6.3557.939 1.00 50.09 D C

ATOM 9129O ALAD 220-13.381-6.4598.657 1.00 51.09 D O

ATOM 9130N LEUD 221-11.155-6.5228.393 1.00 49.73 D N

ATOM 9131CA LEUD 221-10,900-6.8679.784 1.00 49.08 D C

ATOM 9132CB LEUD 221-9,794 -7.9299.872 1.00 50.15 D C

ATOM 9133CG lEUD 221-10.043-9.2399.110 1.00 51.50 D C

ATOM 9134CD1LEUD 221-8.822 -10.1609.246 1.00 52.66 D C

ATOM 9135CD2LEUD 221-11.303-9.9219.638 1.00 50.57 D C

ATOM 9136C LEUD 221-10.524-5.66310.635 1.00 48.60 D C

ATOM 91370 LEUD 221-10,831-5.62411.824 1.00 47.81 D O

ATOM 9138N METD 222-9.846 -4.68910.033 1.00 48.85 D N

ATOM 9139CA METD 222-9.445 -3.48510.754 1.00 48.82 D C

ATOM 9140CB METD 222-8.490 -2.6389.892 1.00 52.88 D C

ATOM 9141CG METD 222-8.043 -1.28310.497 1.0D 55.49 D C

ATOM 9142SD MET1 222-6.945 -1.37811.974 1.00 62.58 D S
D

ATOM 9143CE MET; 2225.308 -1.66111.208 1.00 59.82 D C
D

ATOM 9144C MET' 222-10.693-2,67511.084 1.00 47.06 D C
D

ATOM 9145O MET. 222-10.764-2.02612.120 1.00 46.29 D O
D

ATOM 9146N TYR! 223-11.683-2.74610.204 1.00 45.55 D N
D

ATOM 9147CA TYR; 223-12.918-1.99410.375 1.00 46.04 D C
D

ATOM 9148CB TYRD 223-13.184-1.1899.098 1.00 43.00 D C

ATOM 9149CG TYRD 223-12.142-0,1108.895 1.00 41,68 D C

ATOM 9150CD1TYRD 223-11.9460,876 9.862 1.00 41.07 D C

ATOM 9151CE1 TYRD 223-10.9_561.843 9.779 1.00 41.91 D C

ATOM 9152CD2 TYRD 223-11.320-0.099 7.768 1.00 41.27 D C

ATOM 9153CE2 TYRD 223-10.3260.864 _ 7.6111.00 40.08 D C

ATOM 9154CZ TYRD 223-10.1491.829 8.590 1.00 40.80 D C

ATOM 9155OH TYRD 223-9.1662.782 8.465 1.00 41,38 D O

ATOM 9156C TYRD 223-14.142-2.828 10.7641.00 47.22 D C

ATOM 9157O TYRD 223-15.274-2.540 10.3451.00 46.59 D O

ATOM 9158N ASND 224-13.897-3.852 11.5781.00 47.83 D N

ATOM 9159CA ASND 224-14.935-4.749 12,0741.00 48.77 D C
~

ATOM 9160CB ASND 224-15.369-4.282 13.4601.00 48.77 D C

ATOM 9161CG ASND 224-14.202-4.196 14.4251.00 50.47 D C

ATOM 9162ODi ASND 224-13.481-5.178 14.6461.00 49.64 D O

ATOM 9163ND2 ASND 224-14.002-3.015 15.0051.00 51.51 D N

ATOM 9164C ASND 224-16.153-4.903 11.1581.00 49,24 D C

ATOM 9165O ASND 224-17.297x.727 11.5851.00 48.83 D O

ATOM 9166N ASPD 225-15.880-5.228 9.899 1.00 49 D N

ATOM 9167CA ASPD 225-16.893-5.449 8.872 1.00 . D C
51.05 ATOM 9168CB ASPD 225-17.593-6.785 9.133 1.00 54.37 D C

ATOM 9169CG ASPD 225-16.653-7.879 8.961 1.00 56,91 D C

ATOM 9170OD1 ASPD 225-16.230-8.245 7.813 1.00 56.99 D O

ATOM 9171OD2 ASPD 225-16.335-8.645 9.976 1.00 58 D O

ATOM 9172C ASPD 225-17.935-4.355 8.652 1.00 . D C

ATOM 9173O ASPD 225-18:868-4.532 7,872 1.00 . D O
50.68 ATOM 9174N SERD 226-17.767-3.212 9.305 1.00 50 D N

ATOM 9175CA SERD 226' -18.725-2.120 9.153 1.00 . D C
49.73 ATOM 9176CB SERD 226-19.057-1.537 10.5291.00 50.04 D C

ATOM 9177OG SERD 226I -19.418-2.562 11.4461.00 51.85 D O

ATOM 9178C SERD 226-18.196-1.013 8.236 1.00 47.65 D C

ATOM 9179O SERD 226-17.230-0.330 8.570 1.00 47.60 D O

ATOM 9180N SERD 227-18.833-0.839 7.083 1.00 46 D N

ATOM 9181CA SERD 227-18.4230.197 6.131 1.00 . D C

ATOM 9182CB SERD 227-18.8211.580 6.661 1.00 . D C
44.42 ATOM 9183OG SERD 227-20.2241.744 6.660 1.00 43.62 D O

ATOM 9184C SERD 227-16.9150.159 5.889 1.00 43.31 D C

ATOM 9185O SERD 227-16.2281.162 6.048 1.00 42.26 D O

ATOM 9186N VALD 228-16.417-1.011 5.503 1.00 42.14 D N

ATOM 9187CA VALD 228-14.993-1.221 5.264 1.00 40.03 D C

ATOM 9188CB VALD 228-14.736-2.645 4.663 1.00 41.33 D C

ATOM 9189CG1 VALD 228-13.242-2.914 4.575 1.00 40 D C

ATOM 9190CG2 VALD 228-15.427-3.719 5.522 1.00 . D C
41.49 ATOM 9191C VALD 228-14.364-0.165 4.342 1.00 37.88 D C

ATOM 9192O VALD 228-13.5520.650 4.791 1.00 36.02 D O

ATOM 9193N LEUD 229-14.738-0.198 3.063 1.00 35.58 D N

ATOM 9194CA LEUD 229-14.2220.732 2,065 1.00 34 D C

ATOM 9195CB LEUD 229-14.9110.506 0.723 1.00 . D C
36.40 ATOM 9196CG LEUD 229-14.625-0.813 0.001 1.00 37.06 D C

ATOM 9197CD1 LEUD 229-15.516-0.887 -1.2241.00 37 D C

ATOM 9198CD2 LEUD 229-13.145-0.904 -0.3921.00 . D C

ATOM 9199C LEUD 229-14.3732.193 2.454 1.00 . D C
34.68 ATOM 9200O LEUD 229-13.4332.978 2.331 1 34 D O

ATOM 9201N GLUD 230-15.5522.561 2.934 . . D N
1.00 33.89 ATOM 9202CA GLUD 230-15.7883.940 3.313 1.00 33.09 D C

ATOM 9203CB GLUD 230-17.2524.126 3.696 1.00 33.67 D C

ATOM 9204CG GLUD 230-18.2313.892 2.542 1.00 36 D C

ATOM 9205CD GLUD 230-18.3472.425 2.139 1.00 . D C
36.73 ATOM 9206OE1 GLUD 230-18.2991.549 3.030 1.00 38.27 D O

ATOM 9207OE2 GLUD 230-18.5062.146 0.935 1.00 37,40 D O

ATOM 9208C GLUD 230-14.8654.428 4.436 1.00 32 D C

ATOM 9209O GLUD 230-14.4085.579 4.418 1.00 . D O

ATOM 9210N ASND 231-14.5933.569 5.415 1,00 . D N

ATOM 9211CA ASND 231-13.7113.947 6.521 1.00 . D C
29,62 ATOM 9212CB ASND 231-13.7422.901 7,647 1.00 30 D C

ATOM 9213CG ASND 231-14.8743.129 8.630 1.00 . D C

ATOM 9214OD1 ASND 231-14.8044.014 9.490 1.00 . D 0 30.62 ATOM 9215ND2 ASND 231-15.9362.337 8.497 1 30 D N

ATOM 9216C ASND 231-12.2984.045 5 . , D

. . . C
ATOM 9217O ASND 231-11.5274.888 6.384 1.00 27 D O

ATOM 9218N HISD 232-11.9693.170 5.041 1.00 . D N
26.54 ATOM 9219CA HISD 232-10.6513.185 4.451 1.00 28 D C

ATOM 9220CB HISD 232-10.4271.924 3 1 . D

. . . C
ATOM 9221CG HISD 232-9.0531.833 3 t 3 . . 0.06 D C
ATOM 9222CD2 HISD 232-8.6251 1 . . 1.00 29.18 D C
ATOM 9223NDi HISD 232-7 2 . . 3.761 1.00 28.51 D N
ATOM 9224CE1 HISD 2326.853 - 1.877 3.024 1.00 30.20 D C

ATOM 9225NE2 HISD 232-7.2541.431 1 1 29 D

. . . N
ATOM 9226C HISD 232-10.4384 3 . . 1.00 27.81 D C

. . 3.593 1.00 30.29 D O

-11.4484.804 2.797 1.00 27.76 D N

ATOM 9229CA HISD 233-11,3205.974 1,922 1 27 D C

ATOM 9230CB HISD 233-12.6076.224 1 . , . . 26.79 D C
ATOM 9231CG HISD 233-12.9965 0 . . 1.00 26.71 D C

. . -0.0791.00 25.74 D C

- 4.389 -0.5301.00 29.02 D N
.

ATOM 9234CE1 HISD 233-12.7063.489 -1.2661 26 D C

ATOM 9235NE2 HISD 233-13.9993 -1 . .

. . .00 26.81 D N

. 7.205 2.755 1.00 26.42 D C

i 9237O HIS D 233-10.1788.016 2.384 1.00 24.47 D O
ATOM

ATOM9238N LEU D 234-11.7067.336 3.884 1.00 27.22 D N

ATOM9239CA LEU D 234-11.5128.463 4.778 1.00 27.72 D C

ATOM9240CB LEU D 234-12.5468.420 5.897 1.00 28.25 D C

ATOM9241CG LEU D 234-13.9738.873 5.579 1.00 30.07 D C

ATOM9242CD1LEU D 234-14.9308.293 6.612 1.00 26.93 D C

ATOM9243CD2LEU D 234-14.03110.4025.569 1.0D 28.47 D C

ATOM9244C LEU D 234-10.1148.469 5.399_ 1.00 29.26 D C

ATOM9245O LEU D 234-9.4369.507 5.429 1.00 28.82 D O

ATOM9246N ALA D 235-9.6947.311 5.904 1.00 27.25 D N

ATOM9247CA ALA D 235-8.3967.203 6.553 1.00 28.61 D C

ATOM9248CB ALA D 235-8.1845.777 7.117 1.00 27.43 D C

ATOM9249C ALA D 235-7.2707.567 5.595 1.00 27.31 D C

ATOM9250O ALA D 235-6.4148.365 5.938 1.00 25.22 D O

ATOM9251N VAL D 236-7.2706.980 4.401 1.00 28.01 D N

ATOM9252CA VAL D 236-6.2297.292 3.424 1.00 28.11 D C

ATOM9253CB VAL D 236-6.3846.406 2.166 1.00 27.79 D C

ATOM9254CG1VAL D 236-5.4586.896 1.044 1.00 27.35 D C

ATOM9255CG2VAL D 236-6.0344.965 2.518 1.00 25.68 D C

ATOM9256C VAL D 236-6.2588.790 3.041 1.00 29.55 D C

ATOM9257O VAL D 236-5.2219.461 3.030 1.00 29.24 D O

ATOM9258N GLY D 237-7.4549.313 2.767 1.00 _28.25D N

ATOM9259CA GLY D 237-7.59010.7092.396 1.00 27.38 D C

ATOM9260C GLY D 237-6.96511.6723.383 1.00 27.45 D C

ATOM9261O GLY D 237-6.25212.5972.996 1_.00 27.22 D O

ATOM9262N PHE D 238-7.24711.4604.664 1.00 27.89 D N

ATOM9263CA PHE D 238-6.71212.2915.734 1.00 27.00 D C

ATOM9264CB PHE D 238-7.43811.9897.046 1.00 26.15 D C

ATOM9265CG PHE D 238-8.78012.6377.162 1.00 27.36 D C

ATOM9266CD1PHE D 238-8.88814.0137.278 1.00 26.35 D C

ATOM9267CD2PHE D 238-9.94311.8677.176 1.00 27.79 D C

ATOM9268CE1PHE D 238-10.13314.6267.409 1.00 27.51 D C

ATOM9269CE2PHE D 238-11.19812.4717.308 1.00 28.37 D C

ATOM9270CZ PHE D 238-11.29113.8507.424 1.00 28.23 D C

ATOM9271C PHE D 238-5.23112.0125.939 1.00 27.26 D C

ATOM9272O PHE D 238-4.46112.8976.283 1.00 26.46 D O

ATOM9273N LYS D 239-4.85810.7555.744 1.00 28.48 D N

ATOM9274CA LYS D 239-3.49410.2945.938 1.00 28.23 D C

ATOM9275CB LYS D 239-3.4528.774 5.781 1.00 29.71 D C

ATOM9276CG LYS D 239-2.1058.181 6.023 1.00 31.55 D C

ATOM9277CD LYS D 239-1.6418.545 7.416 1.00 33.79 D C

ATOM9278CE LYS D 239-0.2178.136 7.615 1.00 34.69 D C
ATOM9279NZ LYS D 2390.192 8.460 8.990 1.00 36.28 D N

ATOM9280C LYS D 239-2.51910.9514.971 1.00 27.65 D C

ATOM9281O LYS D 239-1.40211.2905.345 1.00 27.72 D O

ATOM9282N LEU D 240-2.95611.1383.730 1.00 27.67 D N

ATOM9283CA LEU D 240-2.13411.7552.704 1.00 26.91 D C

ATOM9284CB LEU D 240-2.82911.6531.354 1.00 28.10 D C

ATOM9285CG LEU D 240-3.00310.2180.855 1.00 27.86 0 C

ATOM9286CD1LEU D 240-3.72110.250-0.469 1.00 28.41 D C

ATOM9287CD2LEU D 240-1.6369.537 0.712 1.00 28.92 D C

ATOM9288C LEU D 240-1.81113.2043.021 1.00 27.71 D C

ATOM9289O LEU D 240-0.85313.7652.491 1.00 29.36 D O

ATOM9290N LEU D 241-2.60813.8203.883 1.00 26.53 D N

ATOM9291CA LEU D 241-2.34015.1854.268 1.00 25.71 D C

ATOM9292CB LEU D 241-3.42615.7005.225 1.00 26.29 D C
ATOM9293CG LEU D 241-4.83716.0004.683 1.00 27.84 D C

ATOM9294CD1LEU D 241-5.79116.2755.853 1.00 26.26 D C
.

ATOM9295CD2LEU D 241-4.78417.2063.744 1.00 27.46 D C

ATOM9296C LEU D 241-0.98115.2244.971 1.00 25.68 D C

ATOM9297O LEU D 241-0.40316.2865.134 1.00 24.45 D O

ATOM9298N GLN D 242-0.46614.0655.375 1.00 26.80 D N

ATOM9299CA GLN D 2420.815 14.0126.084 1.00 27.98 D C

ATOM9300CB GLN D 2420.774 12.9057.143 1.00 31.08 D C

ATOM9301CG GLN D 242-0.14213.1928.331 1.00 34.61 D C

ATOM9302CD GLN D 242-0.46511.9229.100 1.00 40.41 D C

ATOM9303OE1GLN D 2420.391 11.0499.243 1.00 42.73 D O

ATOM9304NE2GLN D 242-1.69911.8099.599 1.00 42.31 D N

ATOM9305C GLN D 2422.060 13.8265.207 1.00 27.68 D C

ATOM9306O GLN D 2423.188 13.8135.714 1.00 27.74 D O

ATOM9307N GLU D 2431.873 13.6683.901 1.00 24.70 D N
ATOM9308CA GLU D 2433.023 13.5083.040 1.00 24.44 D C

ATOM9309CB GLU D 2432.628 12.8101.721 1.00 25.14 D C

ATOM9310CG GLU D 2432.317 11.2931.889 1.00 22.40 D C

ATOM9311CD GLU D 2432.347 10.4890.568 1.00 23.95 D C

ATOM9312OE1GLU D 2432.693 11.047-0.494 1.00 22.92 D O

ATOM9313OE2GLU D 2432.029 9.281 0.593 1.00 23.06 D O

ATOM9314C GLU D 2433.657 14.8912.829 1.00 24.35 D C

ATOM9315O GLU D 2433.075 15.9143.187 1.00 22.80 D O

ATOM9316N GLU D 2444.863 14.9282.280 1.00 24.35 D N

ATOM9317CA GLU D 2445.567 16.1992.119 1.00 23.78 D C

ATOM9318CB GLU D 2446.888 15.9731.366 1.00 24.07 D C

ATOM9319CG GLU D 2447.851 17.1521.388 1.00 22.91 D C

ATOM9320CD GLU D 2448.275 17.5392.793 1.00 24.82 D C

ATOM9321OEtGLU D 2448.613 16.6443.597 1.00 26.86 D O

ATOM9322OE2GLU D 2448.292 18.7463.100 1.00 26.04 D O

ATOM 9323C GLUD 2444.755 17.3011.431 1.00 24.060 C

ATOM 9324O GLUD 2444.275 17.1260.313 1.00 22.29D O

ATOM 9325N ASND 2454.623 18.436- 2.1161.00 23.99D N

ATOM 9326CA ASND 2453.904 19.5981.587 1.00 25.28D C

ATOM 9327CB ASND 2454.fi78 20.1790.397 1.00 24.87D C

ATOM 9328CG ASND 2454.272 21.6040.070 1.00 26.16D C

ATOM 9329OD1ASND 2454.472 22.074-1.054 1.00 28.29D O

ATOM 9330ND2ASND 2453.713 22.3061.054 1.00 27.35D N

ATOM 9331C ASND 2452.476 19.2901.137 1.00 24.55D C

ATOM 9332O ASND 2452.016 19.8500.144 1.00 24.62D O

ATOM 9333N CYSD 2461.779 18.4121.861 1.00 24.34D N

ATOM 9334CA CYSD 2460.413 18.0371.502 1.00 23.03D C

ATOM 9335CB CYSD 2460.303 16.5171.372 1.00 22.71D C

ATOM 9336SG CYSD 2461.157 15.814-0.030 1.00 23.92D S

ATOM 9337C CYSD 246-0.661 18.5032.474 1.00 22.65D C

ATOM 9338O CYSD 246-1.839 18.2452.255 1.00 21.33D O

ATOM 9339N ASPD 247-0.278 19.1823.550 1.00 22.96D N

ATOM 9340CA ASPD 247-1.275 19.5964.519 1.00 23.08D C

ATOM 9341CB ASPD 247-0.641 19.7545.901 1.00 25.89D C

ATOM 9342CG ASPD 247-1.685 19.9976.988 1.00 27.96D C

ATOM 9343OD1ASPD 247-2.886 19.8056.678 1.00 26.18D O

ATOM 9344OD2ASPD 247-1.312 20.3628.138 1.00 28.31D O

ATOM 9345C ASPD 247-2.017 20.8754.137 1.00 22.45D C

ATOM 9346O ASPD 247-1.738 21.9524,663 1.00 21.77D O

ATOM 9347N ILED 248-2.976 20.7443.228 1.00 22.70D N

ATOM 9348CA ILED 248-3.749 21.8972.774 1.00 23.59D C

ATOM 9349CB ILED 248-4.704 21.5221.605 1.00 24.12D C

ATOM 9350CG2ILED 248-3.888 21.0690.394 1.00 23.37D C

ATOM 9351CG1ILED 248-5.690 20.4352.042 1.00 22.70D C

ATOM 9352CD1ILED 248-6.721 20.0930.963 1.00 23.12D C

ATOM 9353C ILED 248-4.560 22.5713.885 1.00 24.14D C

ATOM 9354O ILED 248-5.045 23.6873.703 1.00 24.25D O

ATOM 9355N PHED 249-4.696 21.9095.036 1.00 23.52D N

ATOM 9356CA PHED 249-5.437 22.4966.149 1.00 25.19D C

ATOM 9357CB PHED 249-6.364 21.4566.779 1.00 23.39D C

ATOM 9358CG PHED 249-7.327 20.8585.818 1.00 25.28D C

ATOM 9359CDtPHED 249-8.135 21.6735.026 1.00 23.77D C

ATOM 9360CD2PHED 249-7.445 19.4845.702 1.00 25.43D C

ATOM 9361CE1PHED 249-9.040 29.1264.144 1.00 24.50D C

ATOM 9362CE2PHED 249-8.356 18.9314.813 1.00 26.35D C

ATOM 9363CZ PHED 249-9.153 19.7604.033 1.00 24.46D C

ATOM 9364C PHED 249-4.526 23.0567.235 1.00 26.66D C

ATOM 93650 PHED 249-4.994 23.3538.327 1.00 27.83D O

ATOM 9366N GLND 250-3.236 23.2096.939 1.00 27.97D N

ATOM 9367CA GLN~ 250-2.274 23.7097.927 1.00 29.08D C
D

ATOM 9368CB GLND 250-0.860 23.7447.335 1.00 29.19D C

ATOM 9369CG GLND 250-0.669 24.7526,203 1.00 30.56D C

ATOM 9370CD GLND 2500.730 24.6675.576 1.00 32.60D C

ATOM 9371OE1GLND 2501.014 23.7754.762 1.00 28.61p O

ATOM 9372NE2GLND 2501.615 25.5895.975 1.00 31.38D N

ATOM 9373C GLND 250-2.583 25.0748.525 1.00 29.86D C

ATOM 9374O GLND 250-2.160 25.3599.642 1.00 30.51D O

ATOM 9375N ASND 251-3.305 25.9257.803 1.00 29.93D N

ATOM 9376CA ASND 251-3.594 27.2458.351 1.00 30.74D C

ATOM 9377CB ASND 251-3.337 28.3377.310 1.00 29.68D C

ATOM 9378CG ASND 251-1.865 28.5017.008 1.00 31:71D C

ATOM 9379OD1ASND 251-1.037 28.5527.919 1.00 30.64D O

ATOM 9380ND2ASND 251-1.525 28.5795.728 1.00 33.38D N

ATOM 9381C ASND 251-4.960 27.4548.978 1.00 30.74D C

ATOM 93820 ASND 251-5.258 28.5679.394 1.00 30.50D O

ATOM 9383N LEUD 252-5.782 26.4039.050 1.00 30.55D N

ATOM 9384CA LEUD 252-7.098 26.5189.682 1.00 29.81D C

ATOM 9385CB LEUD 252-8.047 25.4009.246 1.00 30.61D C

ATOM 9386CG LEUD 252-8.354 24.9547.817 1.00 31.90D C

ATOM 9387CD1LEUD 252-9.679 24.1997.842 1.00 30.60D C

ATOM 9388CD2LEUD 252-8.433 26.1186.875 1.00 31.08D C

ATOM 9389C LEUD 252-6.900 26.37611.191 1.00 30.08D C

ATOM 9390O LEUD 252-5.980 25.67811.642 1.00 29.04D O

ATOM 9391N THRD 253-7.768 27.01111.975 1.00 29.71D N

ATOM 9392CA THRD 253-7.660 26.91393.432 1.00 28.36D C

ATOM 9393CB THRD 253-8.585 27.91414.138 1.00 27.84D C

ATOM 9394OG1THRD 253-9.945 27.52913.915 1.00 25.40D O

ATOM 9395CG2THRD 253-8.350 29.33613.617 1.00 25.70D C

ATOM 9396C THRD 253-8.061 25.50913.892 1.00 30.05D C

ATOM 9397O THRD 253-8.573 24.69913.093 1.00 32.32D O

ATOM 9398N LYSD 254-7.833 25.21315.171 1.00 28.78D N

ATOM 9399CA LYSD 254-8.193 23.91215.714 1.00 30.45D C

ATOM 9400CB LYSD 254-7.773 23.80717.186 1.00 32.69D C

ATOM 9401CG LYSD 254-8.130 22.47817.866 1.00 33.75D C

ATOM 9402CD LYSD 254-7.434 21.29317.209 1.00 34.33D C

ATOM 9403CE LYSD 254-7.576 20.02418.053 1.00 32.40D C

ATOM 9404NZ LYSD 254-6.978 18.85417.354 1.00 33.36D N

ATOM 9405C LYSD 254-9.699 23.67715.573 1.00 30.45D C

ATOM 9406O LYSD 254-10.11722.59015.180 1.00 29.94D O

ATOM 9407N LYSD 255-10.51024.69415.877 1.00 31.54D N

ATOM 9408CA LYSD 255-11.97024.57715.742 1.00 32.35D C

ATOM9409CB LYS D 255-12.66725.85416.212 1.00 34.33 D C

ATOM9410CG LYS D 255-12.75025.98817.721 1.00 39.23 D C

ATOM9411CD LYS D 255-13.15527.411_ 18.1301.00 42.8D D C

ATOM9412CE LYS D 255-13.23127.57 0 19.6521.00 44.65 D C

ATOM9413NZ LYS D 255-13.36329.01220.054 1.00 45.87 D N

ATOM9414C LYS D 255-12.36224.29414.293 1.00 31.65 D C

ATOM9415O LYS D 255-13.18623.41914.024 1.00 30.86 D O

ATOM9416N GLN D 256-11.76725.02313.352 1.00 30.58 D N

ATOM9417CA GLN D 256-12.08524.78011.951 1.00 29.69 D C

ATOM9418CB GLN D 256-11.38725.79311.051 1.00 28.56 D C

ATOM9419CG GLN D 256-11.89627.21411.186 1.00 29.50 D C

ATOM9420CD GLN D 256-11.09828.17210.324 1.00 31.14 D C

ATOM9421OEtGLN D 256-9.874 28.18810.377 1.00 32.57 D O

ATOM9422NE2GLN D 256-11.78928.9729.520 1.00 35.21 D N

ATOM9423C GLN D 256-11.68423.37011.529 1.00 29.85 D C

ATOM9424O GLN D 256-12.42322.7081D.809 1.00 29.89 D O

ATOM9425N ARG D 257-10.52122.90311.982 1.00 29.61 D N

ATOM9426CA ARG D 257-10.06121.57211.602 1.00 29.23 D C

ATOM9427CB ARG D 257-8.582 21.38411.979 1.00 29.57 D C

ATOM9428CG ARG D 257-7.650 22.23411.113 1.00 30.09 D C

ATOM9429CD ARG D 257-6.171 21.96711.365 1.00 28.38 D C

ATOM9430NE ARG D 257-5.653 22.71012.510 1.00 28.21 D N

ATOM9431CZ ARG D 257-5.265 22.15713.657 1.00 28.37 D C

ATOM9432NH1ARG D 257-5.335 20.83913.834 1.00 26.46 D N
~

ATOM9433NH2ARG D 257-4.788 22.92514.628 1.00 28.57 D N

ATOM9434C ARG D 257-10.91520.47812.219 1.00 28.44 D C

ATOM9435O ARG D 257-11.16519.45311.601 1.00 29.19 D O

ATOM9436N GLN D 258-11.36420.68413.443 1.00 27.97 D N

ATOM9437CA GLN D 258-12.21219.68314.061 1.00 28.91 D C

ATOM9438CB GLN D 258-12.33319.94215.558 1,00 30.00 D C

ATOM9439CG GLN D 258-11.15119.43016.349 1.00 32.89 D C

ATOM9440CD GLN D 258-11.44419.42517.820 1.00 35.36 D C

ATOM9441OE1GLN D 258-11.64520.48718.420 1.00 37.26 D O

ATOM9442NE2GLN D 258-11.49618,23318.415 1.00 32.66 D N

ATOM9443C GLN D 258-13.60119.69013.416 1.00 28.37 D C

ATOM9444O GLN D 258-14.20418.64313.215 1.00 28.12 D O

ATOM9445N SER D 259-14.11120.87113.086 1.00 27.69 D N

ATOM9446CA SER D 259-15.42320.94512.461 1.00 28.97 D C

ATOM9447CB SER D 259-15.88522.40312.401 1.00 30.17 D C

ATOM9448OG SER D 259-17._19322.48011.884 1.00 36.40 D O

ATOM9449C SER D 259-15.37120.32011.056 1.00 27.44 D C

ATOM9450O SER D 259-16.21819.50510.690 1.00 27.64 D O

ATOM9451N LEU D 260-14.35620.68610.282 1.00 25.35 D N

ATOM9452CA LEU D 260-14.19120.1538.936 1.00 25.49 D C

ATOM9453CB LEU D 260-12.91320.7088.313 1.00 25.59 D C

ATOM9454CG LEU D 260-12.51120.1076.967 1.00 28.42 D C

ATOM9455CD1LEU D 260-13.37920.7105.865 1.00 28.95 D C

ATOM9456CD2LEU D 260-11.05020.4096.695 1.00 31.46 D C

ATOM9457C LEU D 260-14.12118.6258.922 1.00 26.16 D C

ATOM9458O LEU D 260-14.80217.9538.122 1.00 25.83 D O

ATOM9459N ARG D 261-13.27718.0929.804 1.00 25.00 D N

ATOM9460CA ARG D 261-13.05116.6619.932 1.00 25.90 D C

ATOM9461CB ARG D 261-12.02616.41411.047 1.00 27.18 D C

ATOM9462CG ARG D 261-11.68014.96711.283 1.00 27.06 D C

ATOM9463CD ARG D 261-10.40614.82112.141 1.00 28.91 D C

ATOM9464NE ARG D 261-10.22713.43412.540 1.00 29.71 D N

ATOM9465CZ ARG D 261-9.819 12.45919.736 1.00 31.51 D C

ATOM9466NH1ARG D 261-9.514 12.71410.475 1.00 31.55 D N

ATOM9467NH2ARG D 261-9.788 11.20712.177 1.00 32.67 D N

ATOM9468C ARG D 261-14.32515.86310.204 1.00 25.99 D C

ATOM9469O ARG D 261-14.58214.8449.569 1.00 26.28 D 0 ATOM9470N LYS D 262-15.11916.32211.157 1.00 27.47 D N

ATOM9471CA LYS D 262-16.35315.63511.484 1.00 28.37 D C

ATOM9472CB LYS D 262-17.04316.33312.663 1.0D 31.12 D C

ATOM9473CG LYS D 262-18.30315.61813.173 1.00 33.46 D C

ATOM9474CD LYS D 262-18.79416.25114.484 1.00 36.19 D C

ATOM9475CE LYS D 262-19.89915.42115.129 1.00 37.49 D C

ATOM9476NZ LYS D 262-19.48614.00015.335 1.00 37.73 D N

ATOM9477C LYS D 262-17.28515.60510.271 1.00 27.29 D C

ATOM94780 LYS D 262-17.84914.5529.926 1.00 26.15 D O

ATOM9479N MET D 263-17.42416.7489.610 1,00 27.37 D N

ATOM9480CA MET D 263-18.30716.8288.450 1.0D 28.50 D C

ATOM9481CB MET D 263-18.38918.264_ 7.9301.00 28.8_9D C

ATOM9482CG MET D 263-18.98819.2238-947 1.00 30.14 D C

ATOM9483SD MET D 263-19.54220.7568.211 1.00 35.13 D S

ATOM9484CE MET D 263-18.22021.9078.671 1.00 32.38 D C

ATOM9485C MET D 263-17.84915.8927.351 1.00 28.47 D C

ATOM9486O MET D 263-18.63515.0976.833 1.00 28.68 D 0 ATOM9487N VAL D 264-16.56815.9737.006 1.00 27.74 D N

ATOM9488CA VAL D 264-16.03015.1135.961 1.00 25.41 D C

ATOM9489CB VAL D 264-14.48415.3345.789 1.0D 26.10 D C

ATOM9490CG1VAL D 264-13.90114.2844.848 1.00 21.75 D C

ATOM9491CG2VAL D 264-14.21316.7565.268 1.00 22.67 D C

ATOM9492C VAL D 264-16.31713.6596.331 1.00 23.74 D C

ATOM9493O VAL D 264-16.81112.8845.508 1.00 23.16 D O

ATOM9494N ILE D 265-16.00213.2937.572 1.00 23.77 D N

ATOM9495CA ILE D 265-16.24411.9328.045 1.00 24.32 D C

ATOM9496CB ILE D 265-15.76511.7579.512 1.00 23.88 D C

ATOM9497CG2ILE D 265-16.29410.44310.093 1.00 22.29 D C

ATOM9498CG1ILE D 265-14.23411.7739.554 1.00 23.72 D C

ATOM9499CD1ILE D 265-13.65311.87010.955 1.00 24.49 D C

ATOM9500C ILE D 265-17.73211.5627.922 1.00 24.68 D C

ATOM9501O ILE D 265-18.06810.5117.402 1.00 26.62 D O

ATOM9502N ASP D 266-18.62012.4288.387 1.00 27.07 D N

ATOM9503CA ASP D 266-20.05912.1588.291 1.00 29.11 D C

ATOM9504CB ASP D 266-20.86813.2888.936 1.00 29.96 D C

ATOM9505CG ASP D 266-20.77813.28910.455 1.00 32.67 D C

ATOM9506OD1ASP D 266-21.01814.36811.045 1.00 33.38 D O

ATOM9507OD2ASP D 266-20.48712.22011.056 1.00 32.29 D O

ATOM9508C ASP D 266-20.50612.0166.842 1.00 29.34 D G

ATOM9509O ASP D 266-21.35711.1766.526 1.00 28.72 D O

ATOM9510N ILE D 267-19.92212.8275.961 1.00 28.29 D N

ATOM9511CA ILE D 267-2_0,29612.7934.557 1.00 27.71 D C

ATOM9512CB ILE D 267-19.75014.0263.792 1.00 27.13 D C

ATOM9513CG2ILE D 267-20.16813.9592.347 1.00 26.37 D C
~

ATOM9514CG1ILE D 267-20.33215.3104.378 1.00 26.90 D C

ATOM9515CD1ILE D 267-19.60816.5573.937 1.0D 26.78 D C

ATOM9516C ILE D 267-19.86311.5373.828 1.00 28.80 D C
!

ATOM9517O ILE D 267-20.65910.9433.107 1.00 30.46 D O

ATOM9518N VAL D 268-18.61611.1144.008 1.00 29.38 D N

ATOM9519CA VAL D 268-18.1479.924 3.304 1.00 29.18 D C

ATOM9520CB VAL D 268-16.6099.830 3.329 1.00 28.63 D C

ATOM9521CGtVAL D 268-16.1518.538 2.683 1.00 26.24 D C

ATOM9522CG2VAL D 268-16.01211.0202.576 1.00 28.21 D C

ATOM9523C VAL D 268-18.7418.614 3.802 1.00 30.22 D C

ATOM9524O VAL D 268-18.9717.699 3.014 1.00 31.10 D O

ATOM9525N LEU D 269-18.9928.506 5.099 1.00 32.75 D N

ATOM9526CA LEU D 269-19.5787.274 5.616 1.00 35.10 D C

ATOM9527CB LEU D 269-19.6867.322 7.146 1.00 33.39 D C

ATOM9528CG LEU D 269-18.3117.283 7.826 1.00 32.71 D C

ATOM9529CD1LEU D 269-18.4107.503 9.332 1.00 31.44 D C

ATOM9530CD2LEU D 269-17.6815.947 7.519 1.00 33.11 D C

ATOM9531C LEU D 269-20.9517.112 4.975 1.00 36.85 D C

ATOM9532O LEU D 269-21.3526.005 4.606 1.00 39.05 D O

ATOM9533N ALA D 270-21.6468.231 4.802 1.00 37.21 D N

ATOM9534CA ALA D 270-22.9718.231 4.197 1.00 37.17 D C

ATOM9535CB ALA D 270-23.5909.618 4.319 1.00 37.55 O C

ATOM9536C ALA D 270-22.9857.785 2.732 1.00 37.56 D C

ATOM9537O ALA D 270-24.0587.646 2.147 1.00 37.54 D O

ATOM9538N THR D 271-21.8207.569 2.123 1.00 37.08 D N

ATOM9539CA THR D 271-21.8177.139 0.723 1.00 37.77 D C

ATOM9540CB THR D 271-20.5507.599 -0.034 1.00 36.60 D C

ATOM9541OG1THR D 271-19.3957.013 0.564 1.00 36.22 D 0 ATOM9542CG2THR D 271-20.4279.121 _0.0_141.00 37.07 D C

ATOM9543C THR D 271-21.9595.625 0.624 1.00 37.47 D C

ATOM9544O THR D 271-22.0845.068 -0.463 1.00 36.90 D O

ATOM9545N ASP D 272-21.9384.970 1.779 1.00 39.98 D N

ATOM9546CA ASP D 272-22.1213.519 1.876 1.00 41.38 D C

ATOM9547CB ASP D 272-21.9593.085 3.335 1.00 42.28 D C

ATOM9548CG ASP D 272-21.9251.572 3.509 1.00 43.83 D C

ATOM9549OD1ASP D 272-22.3260.842 2.573 1.00 44.05 D O

ATOM9550OD2ASP D 272-21.5041.118 4.601 1.00 43.12 D O

ATOM9551C ASP D 272-23.5703.261 1.430 1.00 41.63 D C

ATOM9552O ASP D 272-24.4973.845 1.986 1.00 40.24 D O

ATOM9553N MET D 273-23.7702.414 0.426 1.00 42.91 D N

ATOM9554CA MET D 273-25.1292.136 -0.035 1.00 45.28 D C

ATOM9555CB MET D 273-25.1101.175 -1.235 1.00 47.19 D C

ATOM9556CG MET D 273-24.8281.862 -2.575 1.00 48.58 D C

ATOM9557SD MET D 273-25.9123.302 -2.836 1.00 50.10 D 5 ATOM9558CE MET D 273-27.4882.493 -3.190 1.00 47.57 D C

ATOM9559C MET D 273-26.0221.572 1.076 1.00 45.70 D C

ATOM9560O MET D 273-27.2251.860 1.122 1.00 45.40 D O

ATOM9561N SER D 274-25.4290.788 1.976 1.00 45.59 D N

ATOM9562CA SER D 274-26.1690.197 3.086 1.00 46.17 D C

ATOM9563CB SER D 274-25.219-0.5904.004 1.00 46.68 D C

ATOM9564OG SER D 274-24.4450.268 4.826 1.00 47.32 D O

ATOM9565C SER D 274-26.9021.267 3.904 1.00 46.38 D C

ATOM9566O SER D 274-27.7000.951 4.786 1.00 46.69 D O

ATOM9567N LYS D 275-26.6422.534 3.604 1.00 45.64 D N

ATOM9568CA LYS D 275-27.2803.615 4.334 1.00 45.08 D C

ATOM9569CB LYS D 275-26.2134.525 4.938 1.00 46.71 D C

ATOM9570CG LYS D 275-25.3343.818 5.956 1.00 49.07 D C

ATOM9571CD LYS D 275-24.5794.813 6.827 1.00 50.88 D C

ATOM9572CE LYS D 275-23.6224.098 7.780 1.00 52.57 D C

ATOM9573NZ LYS D 275-24.3163.048 8.583 1.00 52.62 D N

ATOM9574C LYS D 275-28.2344.431 3.472 1.00 44.15 D C
ATOM9575O LYS D 275-28.8925.350 3.957 1.00 42.33 D O

ATOM9576N HIS D 276-28.3164.076 2.196 1.00 43.84 D N

ATOM9577CA HIS D 276-29.1784.787 1.268 1.00 44.82 D C

ATOM9578CB HIS D 276-29.2054.076 -0.072 1.00 45.12 D C

ATOM9579CG HIS D 276-30.1294.711 -1.059 1.00 47.05 D C

ATOM9580CD2HIS D 276-31.3414.324 -1.523 1.00 47.00 D C

ATOM 9581ND1HISD 276-29.8595.925 _-1.6531.00 47.09 D N

ATOM 9582CE1HISD 276-30.8666.258 -2_.4411.00 47.70 D C
_ ATOM 9583NE2HISD 276-31.7785.304 -2.3801.00 47.56_D N

ATOM 9584C HISD 276-30.6094.968 1.747 1.00 45.65 D C

ATOM 9585O HISD 276-31.0646.099 1.947 1.00 46.39 D O

ATOM 9586N METD 277-31.3143.854 1.928 1.00 46.46 D N

ATOM 9587CA METD 277-32.7153.874 2.359 1.00 46.19 D C

ATOM 9588CB METD 277-33.2142.454 2.671 1.00 48.67 D C

ATOM 9589CG METD 277-33.3981.562 1.443 1.00 50.77 D C

ATOM 9590SD METD 277-34.6222.174 0.233 1.00 55.78 D S

ATOM 9591CE METD 277-34.1961.170 -1.2191.00 53.03 D C

ATOM 9592C METD 277-32.9984.779 3.541 1.00 44.70 D C

ATOM 9593O METD 277-33.9415.562 3.490 1.00 43.96 D O

ATOM 9594N ASND 278-32.2024.676 4.605 1.00 44.41 D N

ATOM 9595CA ASND 278-32.4075.530 5.776 1.00 44.11 D C

ATOM 9596CB ASND 278-31.5215.094 6.949 1.00 46.67 D C
ATOM 9597CG ASND 278-32.1283.955 7.767 1.00 49.28 D C

ATOM 9598OD1ASND 278-31.8173.802 8.956 1.00 49.70 D O

ATOM 9599ND2ASND 278-32.9793.146 7.136 1.00 48.54 D N

ATOM 9600C ASND 278-32.0926.986 5.452 1.00 43.54 D C

ATOM 96010 ASND 278-32.7347.908 5.959 1.00 42.33 D 0 ATOM 9602N LEUD 279-31.0867.182 4.609 1.00 42.79 D N

ATOM 9603CA LEUD 279-30.6638.517 4.215 1.00 42.02 D C

ATOM 9604CB LEUD 279-29.4168.410 3.334 1.00 42.63 D C

ATOM 9605CG LEUD 279-28.1859.295 3.522 1.00 41.59 D C

ATOM 9606CD1LEUD 279-27.2039.011 2.400 1.00 38.98 D C

ATOM 9607CD2LEUD 279-28.57610.7393.506 1.00 41.44 D C

ATOM 9608C LEUD 279-31.7999.181 3.433 1.00 41.58 D C

ATOM 9609O LEUD 279-32.10710.3573.635 1.00 39.47 D 0 ATOM 9610N LEUD 280-32.4168.409 2.542 1.00 41.26 D N

ATOM 9611CA LEUD 280-33.5068.909 1.713 1.00 41.57 D C

ATOM 9612CB LEUD 280-33.8807.887 0.637 1.00 40.53 D C

ATOM 9613CG LEUD 280-35.0258.281 -0.3081.00 40.74 D C

ATOM 9614CDtLEUD 280-34.7069.623 -0.9951.00 39.05 D C

ATOM 9615CD2LEUD 280-35.2467.170 -1.3481.00 39.66 D C

ATOM 9616C LEUD 280-34.7369.251 2.529 1.00 42.53 D C

ATOM 9617O LEUD 280-35.39510.2592.268 1.00 43.99 D O

ATOM 9618N ALAD 281-35.0448.414 3.516 1.00 43.14 D N

ATOM 9619CA ALAD 28136.202 8.639 4.369 1.00 43.15 D C

ATOM 9620CB ALAD 281-36.3217.517 5.401 1.00 42.65 D C

ATOM 9621C ALAD 281-36.0769.984 5.071 1.00 43.69 D C

ATOM 9622O ALAD 281-36.99010.8055.023 1.00 43.47 D O

ATOM 9623N ASPD 282-34.93610.2055.723 1.00 44.96 D N

ATOM . CA ASPD 282-34.69111.4556.440 1.00 46.47 D C

ATOM 9625CB ASPD 282-33.31111.4337.098 1.00 49.25 D C

ATOM 9626CG ASPD 282-33.29610.6565.391 1.00 52.41 D C

ATOM 9627OD1ASPD 282-33.7109.479 8.385 1.00 54.72 D O

ATOM 9628OD2ASPD 282-32.86611.2249.419 1.00 55.84 D O

ATOM 9629C ASPD 282-34.79512.6765.532 1.00 46.12 D C

ATOM 9630O ASPD 282-35.23013.7505.970 1.00 45.38 D O

ATOM 9631N LEUD 283-34.38712.5124.274 1.00 44.99 D N

ATOM 9632CA LEUD 283-34.45413.6013.312 1.00 45.27 D C

ATOM 9633CB LEUD 283-33.73213.2272.011 1.00 44.27 D C

ATOM 9634CG LEUD 283-33.70314.3380.952 1.00 45.00 D C

ATOM 9635CD1LEUD 283-32.95115.5271_505 1.00 44.21 D C

ATOM 9636CD2LEUD 283-33.05613.853-0.3381.00 43.05 D C

ATOM 9637C LEUD 283-35.92113.9113.026 1.00 45.64 D C

ATOM 9638O LEUD 283-36.30215.0742.920 1.00 46.17 D 0 ATOM 9639N LYSD 284-36.74212.8682.914 1.00 45.86 D N

ATOM 9640CA LYSD 284-38.16413.0462.653 1.00 46.75 D C

ATOM 9641CB LYSD 284-38.84311.6972.402 1.00 47.61 D C

ATOM 9642CG LYSD 284-38.60211.1431.011 1.00 49.56 D C

ATOM 9643CD LYSD 284-39.3529.838 0,775 1.00 51.55 D C

ATOM 9644CE LYSD 284-39.1919.378 -0.6751.00 52,60 D C

ATOM 9645NZ LYSD 284-39.7428.010 -0.9171.00 54.63 D N

ATOM 9646C LYSD 284-38.82613.7543.823 1.00 47.50 D C

ATOM 9647O LYSD 284-39.65914.6493.633 1.00 46.87 D O

ATOM 9648N THRD 285-38.45013.3565.034 9.00 48.24 D N

ATOM 9649CA THRD 285-39.00013.9746.229 1.00 49.50 D C

ATOM 9650CB THRD 285-38.38813.3677.509 1.00 50.01 D C

ATOM 9651OG1THRD 285-38.60311.9507.521 1.00 50.87 D O
r ATOM 9652CG2THRD 285-39.02213.9828.748 1.00 49.50 D C

ATOM 9653C THRD 285-38.67015.4626.172 1.00 50.37 D C

ATOM 9654O THRD 285-39.49416.3126.510 _ 50.57 D 0 1.00 ATOM 9655N METD 286-37.45815.7795.733 1.00 51.58 D N

ATOM 9656CA METD _286-37.06617.1765.634 1.00 _ D C
--52.48 ATOM 9657CB METD 286-35.60117.3185.244 1.00 53.25 D C

ATOM 9658CG METD 286-35.21118.7765.051 1,00 54.45 D C

ATOM 9659SD METD 286-33.45119.0305.014 1. 57.28 D S

ATOM 9660CE METD 286-33.06618.9636.775 _ 54.11 D C
1.00 ATOM 9661C MET0 286-37.91717.9174.619 1.00 52.30 D C

ATOM 9662O METD 286-38:42818.9964.905 1.00 52.38 D O

ATOM 9663N VALD 287-38.05717.3403.431 1.00 52.42 0 N

ATOM 9664CA VALD 287-38.85717.9542.377 1.00 53.83 D C

ATOM 9665CB VALD _28_7-38.909'17,0491.121 1.00 53.45 D C

I 9666CG1VALD 287-39.79017.6820.046 1 00 52 ~ c' ATOM ~ ~ ~ ~ 30 ~

ATOM 9667CG2VALD 287-37.49816.8200.595 1.00 53.37 D C

ATOM 9668C VALD 287-40.28618.2112.864 1.00 55.06 D C

ATOM 9669O VALD 287-40.81519.315_ 2-727211.00 54.02 D O

ATOM 9670N GLUD 288-40.902__17.1863.450 1.00 56.51 D N

ATOM 9671CA GLUD 288-42.26617.3023.944 1.00 58.31 D C

ATOM 9672CB GLUD 288-42.69115.9914.621 1.00 61.34 D C

ATOM 9673CG GLUD 288-44.15915.9625.058 1.00 66.14 D C

ATOM 9674CD GLUD 288-44.67014.5545.353 1.00 68.43 D C

ATOM 9675OE1GLUD 288-43.97613.8086.088 1.00 69.30 D O

ATOM 9676OE2GLUD 288-45.77014.2054.855 1.00 68.46 D O

ATOM 9677C GLUD 288-42.44318.4874.897 1.00 57.57 D C

ATOM 9678O GLUD 288-43.50419.1124.930 1.00 57.22 D O

ATOM 9679N THRD 289-41.40118.7985.661 1.00 57.07 D N

ATOM 9680CA THRD 289-41.43419.9176.602 1.0D 57.17 D C

ATOM 9681CB THRD 289-41.06619.4588.026 1.00 57.51 D C

ATOM 9682OG1THRD 28939.860 18.6857.982 1.00 56.75 D O

ATOM 9683CG2THRD 289-42.18918.6188.627 1.00 57.42 D C

ATOM 9684C THRD 289-40.44721.0036.170 1.00 57.76 D C

ATOM 9685O THRD 289-39.86321.6996.998 1.00 57.93 D O

ATOM 9686N LYSD 290-40.27321.1374.861 1.00 58.14 D N

ATOM 9687CA LYSD 290-39.35522.1114.275 1.00 58.56 D C

ATOM 9688CB LYSD 290-39.36121.9342,751 1.00 57.55 0 C

ATOM 9689CG LYSD 290-38.62122.9891.963 1.00 57.32 D C

ATOM 9690CD LYSD 290-38.78022.7220.477 1.00 57.16 D C

ATOM 9691CE LYSD 290-38.18723.831-0.363 1.00 55.84 D C

ATOM 9692NZ LYSD 290-38.26423.476-1.799 1.00 55.68 D N

ATOM 9693C LYSD 290-39.66423.5674.634 1.00 59.02 D C

ATOM 96940 LYSD 290-40.80224.0214.502 1.00 59.88 D O

ATOM 9695N LYSD 291-38.64424.2925.085 1.00 59.03 D N

ATOM 9696CA LYSD 291-38.78625.7065.446 1.00 58.86 D C

ATOM 9697CB LYSD 291-38.42525.9246.919 1.00 59.86 0 C

ATOM 9698CG LYSD 291-39.42525.4147.949 1.00 62.32 D C

ATOM 9699CD LYSD 291-38.82125.5529.364 1.00 65.42 D C

ATOM 9700CE LYSD 291-39.78325.15510.498 1.00 66.19 D C

ATOM 9701NZ LYSD 291-40.83626.18110.800 1.00 67.32 D N

ATOM 9702C LYSD 291-37.86226.5794.582 1.00 58.12 D C

ATOM 97030 LYSI 291-36.73226.1854.273 1.00 57.58 D O
D

ATOM 9704N VAL~ 292-38.34427.7604.196 1.00 56.72 D N
D

ATOM 9705CA VALD 29237.553 28.6943.395 1.00 55.46 D C

ATOM 9706CB VALD 292-38.14428.9091.973 1.00 56.08 D C

ATOM 9707CG1VALO 292-38.22327.5801.232 1.00 56.44 D C

ATOM 9708CG2VALD 292-39.51729.5632.064 1.00 55.87 D C

ATOM 9709C VALD 292-37.50130.0414.103 1.00 54.80 D C

ATOM 9710O VALD 292-38.45330.4294.782 1.00 54.68 D O

ATOM 9711N THRD 293-36.39030.7543.934 1.00 54.09 D N

ATOM 9712CA THRD 293-36.20132.0564.569 1.00 53.57 D C

ATOM 9713CB THRD 293-34.69832.3364.820 1.00 54.17 D C

ATOM 9714OG1THRD 293-34.02932.5653.569 1.00 53.44 D O

ATOM 9715CG2THRD 293X4.051 31.1445.527 1.00 53.27 D C

ATOM 9716C THRD 29336.770 33.2293.765 1.00 53.05 D C

ATOM 9717O THRD 293-37.41333.0432.728 1.00 51.22 D O

ATOM 9718N SERD 294-36.52734.4354.279 1.00 52.96 D N

ATOM 9719CA SERD 294-36.96535.6823.657 1.00 52.56 D C

ATOM 9720CB SERD 294-36.25_0_36.8544.334 1.00 53.60 D C

ATOM 9721OG SERD 294-36.61238.0923.758 1.00 58.03 D 0 ATOM 9722C SERD 294-36.58635.5992.180 1.00 51.72 D C
ATOM 9723O SERD 294-37.29736.0951.298 1.00 50.59 D 0 ATOM 9724N SERD 295-35.44034.9701.938 1.00 50.25 D N

ATOM 9725CA SERD 295-34.93334.7330.595 1.00 49.63 D C

ATOM 9726CB SERD 295-33.40834.8030.583 1.00 49.47 D C
ATOM 9727OG SERD 295-32.94135.7601.517 1.00 50.29 D O

ATOM 9728C SERD 295-35.38433.3000.324 1.00 48.93 D C
ATOM 9729O SERD 295-35.37632.4591.223 1.00 50.84 D O
ATOM 9730N GLYD 296-35.78033.010-0.900 1.00 48.03 D N
ATOM 9731CA GLYD 296-36.23731.664-1.195 1.00 47.59 D C
ATOM 9732C GLYD 296-35.22530.545-1.004 1.00 46.40 D C
ATOM 9733O GLYD 296-35.22229.596-1.790 1.00 47.21 D O
ATOM 9734N VALD 297-34.37330.6360.019 1.00 45.04 D N
ATOM 9735CA VALD 297-33.37429.5890.265 1.00 44.87 D C
ATOM 9736CB VALD 297-31.92830.1720.364 1.00 43.86 D C
ATOM 9737CG1VALD 297-31.59730.939-0.903 1.00 _44.55D C
ATOM 9738CG2VALD 297-31.79031.0651,578 1.00 4_2.65D C
ATOM 9739C VALD 297-33.67428.7661.522 1.00 44.26 D C
ATOM 9740O VALD 297-34.22329.2782.507 1.00 43.38 D 0 ATOM 9741N LEUD 298-33.32327.4841.467 1.00 43.99 D N
ATOM 9742CA LEUD 298-33.55326.5742.582 1.00 44.42 D C
ATOM 9743CB LEUD 298-32.83325.2472.376 1.00 45.08 D C
ATOM 9744CG LEUD 298-33.29624.2151.361 1.00 46.69 D C
ATOM 9745CD1LEUD 298-33.23824.785-0.049 1.00 47.68 D C
ATOM 9746CD2LEUD 298-32.39022.9981.490 1.00 47.12 D C
ATOM 9747C LEUD 298-33.09427.1103.921 1.00 44.68 D C
ATOM 9748O LEUD 298-32.00927.6834.051 1.00 44.23 D O
ATOM 9749N LEUD 299-33.93726.8984.919 1.00 45.09 D N
ATOM 9750CA LEUD 299-33.62627.2886.272 1.00 46.08 D C
ATOM 9751CB LEUD 299-34.87827.8326.968 1.00 46.43 D C
ATOM 9752CG LEUD 299-34.77328.3348.413 1.00 46.48 D C

ATOM 9753CD1LEUD 299-34.70_027.148 9.376 1.00 46.05 D C

ATOM 9754CD2LEUD 299-33.56129.254 8.552 1.00 45.59 D C

ATOM 9755C _LEUD 299-33.15326.000 6.942 1.00 46.86 D C

ATOM 9756O LEUD 299-33.91425.041 7.087 1.00 46.74 D O

ATOM 9757N LEUD 300-31.87925.974 7.310 1.00 48.21 D N

ATOM 9758CA LEUD 300-31.2_8524.822 7.975 1.00 49.8 D C

ATOM 9759CB LEUD 300-30.20824.188 7.087 __ _ D C
_ 48.24 1.00 ATOM 9760CG LEUD 300-30.70323.628 5 1,00 46.38 0 C

ATOM 9761CD1LEUD 300-29.53523.022 _ 1.00 46.92 D C
5.007 ATOM 9762CD2LEUD 300-31.77622.580 5.984 1.00 44.85 D C

ATOM 9763C LEUD 300-30.68125.322 9.282 1.00 51.65 D C

ATOM 9764O LEUD 300-29.62725.967 9.299 1.00 52.58 D O

ATOM 9765N ASPD 301-31.37125.028 10.3751.00 53.50 D N

ATOM 9766CA ASPD 301-30.95725.457 11.7021.00 55.98 D C

ATOM 9767CB ASPD 301-32.14625.355 12.6571.00 59.49 D C

ATOM 9768CG ASPD 301-31.71925.410 14.1101.00 63.71 D C

ATOM 9769OD1ASPD 301-32.49824.954 14.9811.00 66.78 D O

ATOM 9770OD2ASPD 301-30.59825.913 14.3801.00 65.54 D O

ATOM 9771C ASPD 301-29.77724.694 12.3081.00 55.65 D C

ATOM 9772O ASPD 301-28.63025.142 12.2591.00 57.45 D O

ATOM 9773N ASN; 302-30.09323.550 12.9051.00 53.55 D N
D

ATOM 9774CA ASNi 302-29.13022.683 13.5731.00 51.19 D C
D

ATOM 9775CB ASN' 302-29.89121.629 14.3521.00 51.39 D C
D

ATOM 9776CG ASND 302-30.78120.806 13.4531.00 51.39 D C

ATOM 9777OD1ASND 302-30.77619.577 13.5051.00 52.82 D O

ATOM 9778ND2ASND 302-31.55021.485 12.6081.00 50.28 D N

ATOM 9779C ASND 302-28.15821.956 12.6431.00 49.63 D C

ATOM 9780O ASND 302-28.42121.779 11.4531.00 48.76 D O

ATOM 9781N TYRD 303-27.05021.502 13.2211.00 47.32 D N

ATOM 9782CA TYRD 303-26.03620.764 12.4771.00 44.90 D C

ATOM 9783CB TYRD 303-24.90820.302 13.4111.00 41.87 D C

ATOM 9784CG TYRD 303-23.93119.340 12.7591.00 38.78 D C

ATOM 9785CDtTYRD 303-22.91319.804 11.9161.00 37.60 D C

ATOM 9786CE1TYRD 303-22.01018.922 11 1 35 D C

ATOM 9787CD2TYRD 303-24.02417.968 . . . O C
12.9831.00 36.55 ATOM 9788CE2TYRD 303-23.12817.077 12.3911.00 36.08 D C

ATOM 9789CZ TYRD 303-22.12117.565 11.5631.00 34.98 D C

ATOM 9790OH TYRD 303-21.23116.693 10.9891.00 33.13 D 0 ATOM 9791C TYRp 303-26.63919:534 11.8171.00 44.16 D C

ATOM 9792O TYRD 303-26.28419.198 10.6931.00 44.54 D 0 ATOM 9793N SERD 304-27.54218.864 12.5241.00 43.53 D N

ATOM 9794CA SERD 304-28.17217.648 12.0171.00 43.68 D C

ATOM 9795CB SERD 304-29.16617.095 13.0491.00 45.23 D C

ATOM 9796OG SERD 304-29.82815.936 12.5611.00 46.50 D O

ATOM 9797C SERD 3D4-28.86617.824 10.6691 42 D C

ATOM 9798O SERD 304-28.76616.957 9.801 . . D O
1.00 43.08 ATOM 9799N ASPD 305-29.57418.932 10.4871.00 42.49 D N

ATOM 9800CA ASPD 305-30.24219.162 9 1 41 D C

ATOM 9801CB ASPD 305-31.30520 . . .

. . . 44.37 D C
ATOM 9802CG ASPD 305-32.51919 10 1 . . . 46.55 D C

. . . 1.00 46.48 D O
ATOM 9804OD2ASPD 305-33.19620.709 10 1 49 D

. . . O
ATOM 9805C ASPD 305-29.18819.576 8 1 40 D

. . . C
ATOM 9806O ASPD 305-29.23919.178 7 1 40 D

. . . O
ATOM 9807N ARGD 306-28.22920 8 1 . . . 38.37 D N

. . . 1.00 37.40 D C

. . . .00 37.88 D C
ATOM 9810CG ARGD 306-26.71723.148 8.684 1.00 40.90 D C

ATOM 9811CD ARGD 306-25.67724.027 9.348 1 43 D C

ATOM 9812NE ARGD 306-26.07125 9 . .

. . . 48.54 D N

. . . 1.00 49.47 D C
ATOM 9814NH1ARGD 306-25.15625.857 7.238 1.00 49.11 D N

ATOM 9815NH2ARGD 306-26.23427.527 8 1 52 D N

ATOM 9816C ARGD 306-26.38319.652 , . . D

. . . C
ATOM 9817O ARGD 306-26.32319.488 5 1 34 D

. . . O
ATOM 9818N ILED 307-25.79718 8 1 . . . 34.36 D N
ATOM 9819CA ILED 307-25.01217 7 1 34 . . . .03 D C
ATOM 9820CB ILED 307-24.34116 8 . . 1.00 32.92 D C

. . . 1.00 32.35 D C

. . . 1.00 33.41 D C

. . 7.420 1.00 31.85 D C
AT

OM 9824C ILED 307-25.85316.709 6.816 1 34 D C

ATOM 9825O ILED 307-25.35616 5 . .

. . . 33.53 D O

, . . 1.00 35.57 D N

. . 6.426 1.00 36.58 D C

. 15.705 7.075 1.00 39.99 D C
A

TOM 9829CG GLND 308-30.36714.697 6,464 1 47 D C

ATOM 9830CD GLND 308-31.70614 7 . .

. . . 52.09 D C

. . 8.388 1.00 53.99 D 0 ATO

M 9832NE2GLND 308-32.77714.936 6.440 1 54 D N

ATOM 9833C GLND 308-28.14516 4 . .

. . 1.00 34.54 D C

. 15.253 4.060 1.00 35.14 D O

ATOM 9835N VALD 309-28.31117.404 4.707 1 32 D N

ATOM 9836CA VALD 309-28.42917 3 . .

. . 1.00 29.86 D C

. . 3.370 1.00 29.40 D C

-25.74720.032 1.950 1.00 28.60 D C

ATOM 9839CG2VALD 309-29.99619.7754.090 1.00 27.68 D C

ATOM 9840C VALD 309-27.12417.6322.612 1.00 28.61 D C

ATOM 9841O VALD 309-27.13317.061_ 1.5201.00 28.50 D O

ATOM 9842N LEUD 310-26.00317.9883.237 1.00 28.55 D N

ATOM 9843CA LEUD 310-24.67617.7632.662 1.00 27.80 D C

ATOM 9844CB LEUD 310-23.58518.2643.613 1.00 27.61 D C

ATOM 9845CG LEUD 310-23.57819.7823.816 1.00 29.64 D C

ATOM 9846CD1LEUD 310-22.45320.2004.788 1.00 28.15 D C

ATOM 9847CD2LEUD 310-23.40020.4612.448 1.00 29.96 D C

ATOM 9848C LEUD 310-24.42216.3072.328 1.00 26,49 D C

ATOM 9849O LEUD 310-23.83716.0061.294 1.00 27.32 D O

ATOM 9850N GLND 311-24.85815.4043.200 1.00 27.12 D N

ATOM 9851CA GLND 311-24.68013.9702.978 1.00 27.37 D C

ATOM 9852CB GLND 311-25.11913.1804.219 1.00 28.28 D C

ATOM 9853CG GLND 311-24.25113.3745.448 1.00 28.52 D C

ATOM 9854CD GLND 311-24.54712.7096.669 1.00 31.48 D C

ATOM 9855OEiGLND 311-26.04812.8366.917 1.00 33.86 D O

ATOM 9856NE2GLND 311-24.01912.0067.449 1.00 28.43 D N

ATOM 9857C GLND 311-25.50213.5291.765 1.00 27.68 D C

ATOM 9858O GLND 311-25.00412.8410.886 1.00 27.77 D O

ATOM 9859N ASND 312-26.77013.9231.717 1.00 29.25 D N

ATOM 9860CA ASND 312-27.61013.5630.577 1.00 28.37 D C

ATOM 9861CB ASND 312-29.05814.0010.827 1.00 30.05 D C

ATOM 9862CG ASND 312-29.81613.0091.678 1.00 30.66 D C

ATOM 9863OD1ASND 312-30.17711.9381.215 1.00 30.59 D O

ATOM 9864ND2ASND 312-30.03613.3512.935 1.00 31.69 D N

ATOM 9865C ASND 312-27.05114.230-0.6791.00 27.23 D C

ATOM 9866O ASND 312-27.04913.641-1.7601.00 27.19 D O

ATOM 9867N METD 313-26.55415.453-0.5341.00 25.96 D N

ATOM 9868CA METD 313-25.98616.141-1.6561.00 25.76 D C

ATOM 9869CB MET, 313-25.50917.540-1.3041.00 25.45 D C
D

ATOM 9870CG METD 313-24.93418.291-2.4961.00 26.46 D C

ATOM 9871SD METD 313-24.17019.836-2.0661.00 26.86 D S

ATOM 9872CE METD 313-25.55220.728-1.4421.00 24.47 D C

ATOM 9873C METD 313-24.82115.378-2.3241.00 25.11 D C

ATOM 9874O METD 313-24.80515.158-3.5361.00 26.21 D O

ATOM 9875N VALD 314-23.84514.962-1.5221.00 25.48 D N

ATOM 9876CA VALD 314-22.70114.240-2.0881.00 24.66 D C

ATOM 9877CB VALD 314-21.55014.082-1.0691.00 24.42 D C

ATOM 9878CGtVALD 314-20.39913.289_ 1.00 23.88 D C
1.697 ATOM 9879CG2VALD 314-21.06815.450-0.6201.00 22.96 D C

ATOM 9880C VALD 314-23.12812.869-2.5601.00 24.52 D C

ATOM 9881O VALD 314-22.57912.323-3.5301.00 24.33 D O

ATOM 9882N HISD 315-24.11312.314-1.8611.00 26.20 D N

ATOM 9883CA HISD 315-24.65011.000-2.1941.00 27.14 D C

ATOM 9884CB HISD 315-25.64310.556-1.0991.00 28 D C

ATOM 9885CG HISD 315-26.2679.214 -1.3441.00 . D C
31.79 ATOM 9886CD2HISD 315-27.5538.798 -1.2431.00 32.15 D C

ATOM 9887ND1HISD 315-25.5438.116 -1.7561.00 32.50 D N

ATOM 9888CE1HISD 315-26.3567.085 -1.9061.00 33.96 D C

ATOM 9889NE2HISD 315-27.5817.472 -1.6001.00 33.98 D N
ATOM 9890C HISD 315-25.31511.114-3.5681.00 27.26 D C

ATOM 9891O HISD 315-25.19910.213-4.3981.00 27.44 D O
ATOM 9892N CYSD 316-25.99112,233-3.8251.00 27.77 D N

ATOM 9893CA CYSD 316-26.62312.425-5.1351.00 28.34 D C

ATOM 9894CB CYSD 316-27.46913.708-5.1571.00 29.87 D C
ATOM 9895SG CYSD 316-29.07713.620-4.3171.00 30 D S

ATOM 9896C CYSD 316-25.54512.535-6.2161.00 . D C
ATOM 9897O CYSD 316-25.64911.934-7.2941.00 28.00 D O
28.60 ATOM 9898N ALAD 317-24.51313.321-5.9241.00 27.50 D N
ATOM 9899CA ALAD 317-23.42613.523-6.8621.00 26.86 D C
ATOM 9900CB ALAD 317-22.38814.491-6.2691.00 25.99 D C
ATOM 9901C ALAD 317-22.79212.178-7.2061.00 28.31 D C
ATOM 9902O ALAD 317-22.45711.924-8.3611.00 29.25 D O
ATOM 9903N ASPD 318-22.64811.309-6.2091.00 30.42 D N
ATOM 9904CA ASPD 318-22.0579.991 -6.4171.00 31.25 D C
ATOM 9905CB ASPD 318-21.8019.338 -5.0481.00 32.94 D C
ATOM 9906CG ASPD 318-20.9248.083 -5.1221.00 32.82 D C
ATOM 9907OD2ASPD 318-21.2827.111 -4.4381.00 37.47 D O
ATOM 9908C ASPD 318-22.9759.124 -7.2851.00 32.18 D C
ATOM 9909O ASPD 318-22.5098.268 -8.0391.00 30.83 D 0 ATOM 9910OD1ASPD 318-19.8758.047 -5.8121.00 33.58 D O
ATOM 9911N LEUD 319-24.2849.346 -7.1921.00 33.65 D N
ATOM 9912CA LEUD 319-25.2268.574 -8.0011.00 33.82 D C
ATOM 9913CB LEUD 319-26.3347.984 -7.1291.00 34.12 D C
ATOM 9914CG LEUD 319-25.9317,130 -5.9251.00 34.70 D C
ATOM 9915CD1LEUD 319-27.1616.402 -5.4241.00 34.83 D C
ATOM 9916CD2LEUD 319-24.8586.133 -6.3051.00 34.77 D C
ATOM 9917C LEUD 3i9-25.8409.487 -9.0531.00 34.40 D C
ATOM 9918O LEUD 319-27.0629.487 -9.2721.00 34.80 D O
ATOM 9919N SERD 320-24.98110.251-9.7201.00 33.52 D N
ATOM 9920CA SERD 320-25.43311.199-10.7211.00 32.26 D C
ATOM 9921CB SERD 320-24.75912.557-10,4771.00 33.11 D C
ATOM 9922OG SERD 320-23.38012.500-10.8101.00 30.69 D O
ATOM 9923C SERD 320-25.20910.795-12.1701.00 32.82 D C
ATOM 9924O SERD 320-25.77911.427-13.0701.00 33.46 D O

ATOM 9925N ASN 321 9.763 _ -12.4261.00 31.75 D N
D -24.403 ATOM 9926CA ASN 321 9.402 -13.8161.00 33.04 D C
D -24.167 ATOM 9927CB ASN 321-23.1148.267 -13.9571.00 33.15 D C
D

ATOM 9928CG ASND 321-23.4946.982 -13.2421.00 35.89 D C

ATOM 9929OD1ASND 321-24.32$6.206 -13.7221.00 36.04 D O

ATOM 9930ND2ASND 321-22.8756.743 -12.0841.00 36.13 D N

ATOM 9931C ASND 321-25.4559.108 -14.6041.00 32.96 D C

ATOM 9932O ASND 321-25.5449.448 -15.7731.00 31.96 D O

ATOM 9933N PROD 322-26.4868.518 -13.9661.00 34.20 D N

ATOM 9934CD PROD 322-26.5897.891 -12.6391.00 33.33 D C

ATOM 9935CA PROD 322-27.6988.261 -14.7561,00 34.00 D C

ATOM 9936CB PROD 322-28.5387.356 -13.8441.00 33.11 D C

ATOM 9937CG PROD 322-27.5356.741 -12.9251.00 34.43 D C

ATOM 9938C PROD 322-28.4489.557 -15.1091.00 34.95 D C

ATOM 9939O PROD 322-29.4259.520 -15.8651.00 35.13 D O

ATOM 9940N THR0 323-27_.99910.696 -14.5731.00 33.79 D N

ATOM 9941CA THRD 323-28.67111.964 -14.S6D1.00 32.29 D C

ATOM 9942CB THRD 323-29.01912.744 -13.5591.00 32.90 D C

ATOM 9943OG1THRD 323-27.82113.256 -12.9461.00 31.35 D O

ATOM 9944CG2THRD 323-29.75411.835 -12.5821.00 30 D C

ATOM 9945C THRD 323-27.86912.892 -15.7741.00 . D C
33.42 ATOM 9946O THRD 323-28.27314.028 -16.0231.00 33.42 D O

ATOM 9947N LYSD 324-26.74312.403 -16.2821.00 33.20 D N

ATOM 9948CA LYSD 324-25.88813.198 -17.1621.00 33.21 D C

ATOM 9949CB LYSD 324-24.41512.798 -16.9471 30 D C

ATOM 9950CG LYSD 324-23.91212.918 -15.497. . D C
1.00 30.96 ATOM 9951CD LYSD 324-23.88614.366 -15.0361.00 30.55 O C

ATOM 9952CE LYSD 324-23.45614.520 -13.5821.00 30.95 D C

ATOM 9953NZ LYSD 324-21.98614.428 -13.3871.00 31.45 D N

ATOM 9954C LYSD 324-26.28512.959 -18 1 34 D C

ATOM 9955O LYSD 324-27.08712.077 . . . D O
-18.9201.00 33.96 ATOM 9956N PROD 325-25.75013.762 -19.5681.00 35.88 D N

ATOM 9957CD PROD 325-24.89914.961 -19.4571.00 35.84 D C

ATOM 9958CA PROD 325-26.12213.516 -20.9621.00 36.04 D C

ATOM 9959CB PROD 325-25.18714.437 -21.7321 35 D C

ATOM 9960CG PROD 325-25.06415.603 -20 . . D C

ATOM 9961C PROD 325-25.84412.037 . . . D C
-21.2271.00 37.30 ATOM 9962O PROD 325-24.85011.490 -20 1 35 D O

ATOM 9963N LEUD 326-26.72911 , . .

. . . 8.10 D N
ATOM 9964CA LEUD 326-26.6269 -22 1 . . . 39.19 D C
ATOM 9965CB LEUD 326-27.6529 -23 1 . . . 39.65 D C
ATOM 9966CG LEUD 326-27.6708 -23 1 . . . 41.86 D C
ATOM 9967CD1LEUD 326-28.1797 -22 1 . . . 42.25 D C
ATOM 9968CD2LEUD 326-28.5587 -24 1 . . . 43.09 D C
ATOM 9969C LEUD 326-25.2379 -22 1 . . . 39.14 D C
ATOM 99700 LEUD 326-24.7768 -22 1 . . . 40.22 D O
ATOM 9971N GLND 327-24.57210 -23 1 . . . 38.64 D N
ATOM 9972CA GLND 327-23.23110 -23 1 . . . 39.38 D C
ATOM 9973CB GLND 327-22.67111 -24 1 . . . 41.58 D C

. . - 1.00 47.27 D C
ATOM 9975CD GLND 327-20 12 , . . . 1.00 49.86 D C

. . . 1.00 50.03 D O

. . -26.1291.00 51,87 D N

ATOM 9978C GLND 327-22.3079.807 -22.7621 37 D C

ATOM 9979O GLND 327-21.4258 -22 . .

. . . 37.50 D O

. . . 1.00 34.98 D N

. . . 1. 33.93 D C

. . -19.5931.00 32.02 D C
ATO

M 9983CG LEUD 328-20.81112.766 -20.0721 32 D C

ATOM 9984CD1LEUD 328-21.10514.D34 -19 . .

. . 32.00 D C

. . . 1.00 31.85 D C

. . -19.6431.00 32.92 D C
ATOM

99870 LEUD 328-21.3548.374 -19.2001 33 D O

ATOM 9988N TYRD 329-23.4689.097 -19 . .

. . 33.13 D N
ATOM 9989CA TYRD 329-24.0567 -18 . , 1.00 33.57 D C
ATOM 9990CB TYRD 329-25.575$ -18 . . 1.00 33.73 D C

' . . . 1.00 33.75 D C
ATOM 9992CD1TYRD 329-25.8086 -16 . . 1.00 33.26 D C

. . -16.2941.00 34.20 D C

- 6.738 -18.4091.00 35.36 D C
.

ATOM 9995CE2TYRD 329-28.4385.795 -17 1 35 D

. . . C
ATOM 9996CZ TYRD 329-27.8805 -16 . . 1.00 35.36 D C

. . -16.0101.00 36.82 D O

-23.6116.633 -19.2081.00 34.07 D C

ATOM 9999O TYRD 329-23.2555.751 -18 1 34 D

. . . O
ATOM 10000N ARGD 330-23.6306 -20 . . 1.00 35.21 D N

. . -21.1411.00 35.77 D C

-23.5245.223 -22.6471.00 38.33 D C

ATOM 10003CG ARGD 330-25.0065.312 -23 1 41 D

. . . C
ATOM 10004CD ARGD 330-25.3654 -24 . . 1.00 44.41 D C

. . -25.2441.00 47.82 D N

-24.4713.522 -26.2331.00 50.08 D C
AT

OM 10007NH1ARGD 330-25.2252.427 -26.1891 50 D

. . N
ATOM 10008NH2ARGD 330-23.6623 -27 . . 1.00 50.24 D N

. . -2D.9081.00 34.36 D C

330-21.4443.654 -20.8191.00 32.94 D O
' ATOM 10011N GLND 331-20.9075.823 -20.8221.0D 34.88 D N
ATOM 10012CA GLND 331-19.4965.521 -20.5811.00 35.46 D C
ATOM 10013CB GLND 331-18.6296:745 -20.8291.00 34.80 D C
ATOM 10014CG GLND 331-18.6507.166 -22.2701.00 36.38 D C

ATOM 10015CD GLND 331-17.7938.374 -22.5331.00 35.88 D C

ATOM 10016OE1GLND 331-16.5658.299 -22.5161.00 36.04 D O
ATOM 10017NE2GLND 331-18.4379.502 -22.7711.00 36.99 D N
ATOM 10018C GLND 331-19.3345.047 -19.1541.00 35.17 D C

ATOM 10019O GLND 331-18.5564.131 -18.8771.00 35.45 D O

ATOM 10020N TRPD 332-20.0905.668 -18.2561.00 34.71 D N
ATOM 10021CA TRPD 332-20.0605.305 -16.8531.00 35.47 D C
ATOM 10022CB TRPD 332-20.8336.327 -16.0271.00 35.54 D C
ATOM 10023CG TRPD 332-20.1077.630 -15.8671.00 35,29 D C

ATOM 10024CD2TRPD 332-18.8107.821 -15.2901.00 35.10 D C

ATOM 10025CE2TRPD 332-18,5369.209 -15.3311.00 35.50 D C

ATOM 10026CE3TRPD 332-17.8526.957 -14.7401.00 33.59 D C
ATOM 10027CD1TRPD 332-20.5548.869 -16.2251.00 35,14 D C

ATOM 10428NE1TRPD 332-19,6189.822 -15.9081.00 35.38 D N

ATOM 10029CZ2TRPD 332-17.3379.757 -14.8371.00 34.82 D C

ATOM 10030CZ3TRPD 332-16.6617.502 -14.2591.00 33.34 D C
ATOM 10031CH2TRPD 332-16.4188.890 -14.3031.00 32.47 D C

ATOM 10032C TRPD 332-20.6473.918 -16.6421.00 36.52 D C

ATOM 10033O TRPD 332-20.1763.168 -15.7901.00 36.36 D O

ATOM 10034N THRD 333-21.6773.572 -17.4131.00 37.37 D N

ATOM 10035CA THRD 333-22.2862.251 -17.2921.00 37.58 D C

ATOM 10036CB THRD 333-23.6292.157 -18.0711.00 37.61 D C

ATOM 10037OG1THRD 333-24.6662.824 -17.3361.00 37.21 D O

ATOM 10038CG2TNRD 333-24,0350.701 -18.2661.00 37.22 D C

ATOM 10039C THRD 333-21.3361.162 -17.8021.00 37.71 D C

ATOM 10040O THRD 333-21.2490.084 -17.2101.00 36.95 D O

ATOM 10041N ASPD 334-20.6351.437 -18.8971.00 37.77 D N

ATOM 10042CA ASPD 334-19.7060.455 -19.4481.00 40.62 D C

ATOM 10043CB ASPD 334-19.0780.934 -20.7741.00 41,87 D C

ATOM 10044CG ASPD 334-20.0911.073 -21.9111.00 44.41 D C

ATOM 10045OD1ASPD 334-21.1600.414 -21.8811.00 44.69 D O

ATOM 10046OD2ASPD 334-19.7961.840 -22.8571.00 45.39 D O

ATOM 10047C ASPD 334-18.5820.206 -18.4491.00 41.17 D C

ATOM 10048O ASPD 334-18.168-0.931-18.2311.00 42.01 D O

ATOM 10049N ARGD 335-18.0881.284 -17.8501.00 41.48 D N

ATOM 10050CA ARGD 335-17.0031.189 -16.8871.00 41.19 D C

ATOM 10051CB ARGD 335-16.4712,584 -16.5601.00 38.75 D C

ATOM 10052CG ARGD 335-15.5503.146 -17.6301.00 37.77 D C

ATOM 10053CD ARGD 335-15.4304.651 -17.5081.00 36.85 D C

ATOM 10054NE ARGD 335-14.3425.197 -18.3191.00 36.93 D N

ATOM 10055CZ ARGD 335-13.0495.034 -18.0441.00 36.$6 D C

ATOM 10056NH1ARGD 335-12.6764.332 -16.9751.00 34.56 D N

ATOM 10057NH2ARGD 335-12.1275.592 -18.8251.00 34.90 D N

ATOM 10058C ARGD 335-17.4240,476 -15.6131.00 42.00 D C

ATOM 10059O ARGD 335-16.697-0.378-15.1011.00 40.79 D O

ATOM 10060N ILED 336-18.5960.820 -15.0991.00 43.34 D N

ATOM 10061CA ILED 336-19.0550.184 -13.8791.00 45.64 D C

ATOM 10062CB fLED 336-20,3600.835 -13.3481.00 45.69 D C

ATOM 10063CG2ILED 336-21,4720.692 -14.3691.00 47,49 D C

ATOM 10064CG1ILED 336-20.7820.181 -12.0281.00 45.60 D C

ATOM 10065CD1ILED 336-19.9360.559 -10.8461.00 44.64 D C

ATOM 10066C ILED 336-19.266-1.307-14.1371.00 47.26 D C

ATOM 10067O ILED'336-18,844-2,134-13.3331.00 48.05 D O

ATOM 10068N METD 337-19.893-1,660-15.2591.00 48.52 D N

ATOM 10069CA METD 337-20.113-3.073-15.5531.00 50.60 D C

ATOM 10070CB METD 337-20.973-3.265-16.8071.00 51.17 D C

ATOM 10071CG METD 337-22.388-2.693-16.7381.00 52,96 D C
ATOM 10072SD METD 337-23.3583,137 -15.2841.00 55.48 D S
ATOM 10073CE METD 337-23.385-4.946-15.3981.00 55.22 D C

ATOM 10074C METD 337-18.787-3.804-15.742_1.00 51.48 D C

ATOM 10075O METD 337-18.634x.932 -15.2901.00 52.21 D O

ATOM 10076N GLUD 338-17.826-3.171-16.4071.00 52.82 D N

ATOM 10077CA GLUD 338-16.5353.814 -16.617_ 54.35 D C
1.00 ATOM 10078CB GLUD 338-15.585-2.904-17.4021.00 54.26 D C

ATOM 10079CG GLUD 338-14.239-3.565-17.6931.00 55.84 D C

ATOM 10080CD GLUD 338-13.243-2.650-18.3941.00 57.46 D C

ATOM 10081OE1GLUD 338-13.586_-2,086-19.4571.00 59.14 D O
ATOM 10082OE2GLUD 338-12.109-2.502-17.8871.00 57.89 D O

ATOM 10083C GLUD 338-15.889-4.166-15.2801.00 56.18 D C

ATOM 10084O GLUD 338-15.133-5.132-15.1771.00 56.96 D O

ATOM 10085N GLUD 339-16.186-3.372-14.2551.00 56.90 D N

ATOM 10086CA GLUD 339-15,6233.600 -12.9351.00 57.30 D C

ATOM 10087CB GLUD 339-15.619-2.294-12.1411.00 57.14 D C

ATOM 10088CG GLUD 339-14.876-2.371-10.8291.00 56.31 D C

ATOM 10089CD GLUD 339-14.833-1.041-10.1201.00 56.16 D C

ATOM 10090OE1GLUD 339-14.403-0.054-10.7521.00 55.60 D O

ATOM 10091OE2GLUD 339-15.225-0.985_ 1.00 56,48 D O
-8.936 ATOM 10092C GLUD 339-16.419-4.670-12.1951.00 57.96 D C

ATOM 10093O GLUD 339-15.855-5.481-11 1.00 58.03 D O
.463 ATOM 10094N PHED 340-17.732-4.666_ 1.00 58.99 D N
12.386 ATOM 10095CA PHED 340-18.582-5.657-11.7481.00 59.88 D C

ATOM 10096CB PHED 344-20.062-5 -12 1 00 60 D C
I ~ ~ ~ ~ ~ ~ 357 001 57 ATOM10097CG PHED 340-20.622-4.255__-11.1441.00 60.84 D C

ATOM10098CD1PHED 340-20.023-3.915-9.936 1.00 60.82 D C
_ ATOM10099CD2PHED 340-21.791-3.597- -11.5181.00 61.52 D C

ATOM10100CE1PHED 340-20.580-2.938-9.112 1.00 61.11 D C

ATOM10101CE2PHED 340-22.356-2.619-10.7001.00 61.22 D C

ATOM10102CZ PHED 340-21.747-2.291-9.494 1.00 61.00 D C

ATOM10103C PHED 340-18.251-7.031-12.3051.00 60.37 D C

ATOM10104O PHED 340-18.318-8.026-11.5861.00 59.97 D O

ATOM10105N PHED 341-17.898-7.081-13.5891.00 61.11 D N

ATOM10106CA PHED 341-17.553-8.345-14.2321.00 62.68 D C

ATOM10107CB PHED 341-17.681-8.241-15.7551.00 62.90 D C

ATOM10108CG PHED 341-19.092-8.465-16.2331.00 63.61 D C

ATOM10109CD1PHED 341-20.150-8.675-15.5591.00 63.58 D C

ATOM10110CD2PHED 341-19.369-7.296-17.3591.00 64.26 D C

ATOM10111CE1PHED 341-21.463-8.521-15._9971.00 63.80 D C

ATOM10112CE2PHED 341-20.686-7.136-17.8081.00 64.84 D C

ATOM10113CZ PHED 341-21.733-7.750-17.1221.00 64.05 D C

ATOM10114C PHED 341-16.153-8:822-13.8691.00 63.54 D C

ATOM10115O PHED 341-15.851-10.006-13.9901.00 63.08 D O

ATOM10116N ARGD 342-15.292-7.904-13.4441.00 65.01 D N

ATOM10117CA ARGD 342-13.949-8.292-13.0401.00 66.50 D C

ATOM10118CB ARGD 342-13.041-7.069-12.8601.00 68.78 D C

ATOM10119CG ARGD 342-12.739-6.305-14.1461.00 72.79 D C

ATOM10120CD ARGD 342-11.975-7.147-15.1651.00 75.38 D C
~

ATOM10121NE ARGD 342-11.788-6.430-16.4271.00 79.46 D N

ATOM10122CZ ARGD 342-11.241-6.958-17.5231.00 81.25 D C

ATOM10123NH1ARGD 342-10.820-8.220-17.51A1.00 81.99 D N

ATOM10124NH2ARGD 342-11.116-6.226-18.6281.00 81.24 D N

ATOM10125C ARGD 342-14.115-9.005-11.7091.00 66.08 D C

ATOM10126O ARGD 342-13.407-9.960-11.4181.00 66.66 D O

ATOM10127N GLND 343-15.068-8.536-10.9091.00 65.96 D N

ATOM10128CA GLND 343-15.333-9.141-9.610 1.00 66.18 D C

ATOM10129CB GLND 343-16.168-8.208-8.727 1.00 65.61 D C

ATOM10130CG GLND 343-16.438-8.780-7.338 1.00 65.42 D C

ATOM10131CD GLND 343-17.174-7.820-6.423 1.00 65.23 D C

ATOM10132OE1GLND 343-16.771-6.672-6.256 1.00 65.69 D O

ATOM10133NE2GLND 343-18.253-8.294-5.809 1.00 66.00 D N

ATOM10134C GLND 343-16.077-10.458-9.799 1.00 66.51 D C

ATOM10135O GLND 343-15.513-11.434-9.101 1.00 66.79 D O

ATOM10136N GLYD 344-17.009-10.479-10.7461.00 66.43 D N

ATOM10137CA GLYD 344-17.762-11.690-11.0011.00 66.38 D C

ATOM10138C GLYD 344-16.812-12.825-11.3091.00 66.62 D C

ATOM10139O GLYD 344-16.957-13.945-10.8321.0D 66.75 D O

ATOM10140N ASPD 345-15.798-12.526-12.1131.00 67.06 D N

ATOM10141CA ASPD 345-14.799-13.513-12.4901.00 67.53 D C

ATOM10142CB ASPD 345-13.810-12.904-13.4841.00 66.99 D C

ATOM10143CG ASPD 345-14.438-12.628-14.8381.00 66.76 D C

ATOM10144OD1ASPD 345-15.683-12.667-14.9351.00 66.48 D O

ATOM10145OD2ASPD 345-13.688-12.367-15.8031.00 66.40 D O

ATOM10146C ASPD 345-14.060-13.990-11.2481.00 68.51 D C

ATOM10147O ASPD 345-14.058-15.179-10.9351.00 69.36 D O

ATOM10148N ARGD 346-13.440-13.057-10.5341.00 68.92 D N

ATOM10149CA ARGD 346-12.699-13.410-9.331 1.00 69.04 D C

ATOM10150CB ARGD 346-12.144-12.149-8.659 1.00 68.11 D C

ATOM10151CG ARGD 346-11.076-11.432-9._4801.00 67.10 D C

ATOM10152CD ARGD 346-10.704-10.091-8.564 1.00 66.86 D C

ATOM10153NE ARGD 346-10.057-10.223-7.559 1.00 66.50 D N

ATOM10154CZ ARGD 346-9.608 -9.196-6.840 1.00 65.83 D C

ATOM10155NH1ARGD 346-9.737 -7.956-7.294 1.00 64.55 D N

ATOM10156NH2ARGD 346-9.016 -9.408-5.672 1.00 65.93 D N

ATOM10157C ARGD 346-13.571-14.184-8.352 1.0D 69.67 D C

ATOM10158O ARGD 346-13.096-15.091-7.675 1.00 70.07 D O

ATOM10159N GL D 347_-14.851-13_839-8.286 1.00 _ _70.56D N
U

ATOM10160CA _ D 347-15.753-1_4.522-7.370 1.00 72.11 D C
_ GLU

ATOM10161CB _ D 347-17.107-13.810-7.314 1.00 72.04 D C
GLU

ATOM10162CG GLUD 347-17:073-12.487-6.564 1.00 72.01 D C

ATOM10163CD GLUD 347-18.438-11.835-6.469 ~ _1.0072:30 D C

ATOM10164OE1GLUD 347-19.100-11.695-7.521 1.00 _72.3_6_D O

ATOM10165OE2GLUD 347-18.847-11.459-5.347 1.00 71.47 D O

ATOM10166C GLUD 347-15.953-15.991-7.718 1.00 73.10 D C

ATOM10167O GLUD 347-16.092-16.823-6.826 1.00 73.15 D O

ATOM10168N ARGD 348-15.968-16.327-9.003 1.00 74.36 D N

ATOM10169CA ARGD 348-16.149-17.727-9.359 1.00 76.30 D C

ATOM10170CB ARGD 348-16.841-17.873-10.7261.00 76.69 D C

ATOM10171CG ARGD 348-16.018-17.494-11.9431.00 77.68 D C

ATOM10172CD ARGD 348-16.784-17.851-13.2121.00 77.87 D C

ATOM10173NE ARGD 348-17.998-17.052-13.3661.00 78.32 D N

ATOM10174CZ ARGD 348-18.030-15.832-13.8951.00 78.58 D C

ATOM10175NH1ARGD 348-16.913-15.261-14.3291.00 78.28 D N

ATOM10176NH2ARGD 348-19.181-15.178-13.9891.00 78.76 D N

ATOM10177C ARGD 348-14.822-18.486-9.333 1.00 76.97 D C

ATOM10178O ARGD 348-14.804-19.715-9.293 1.00 76.59 D O

ATOM10179N GLUD 349-13.713-17.749-9.336 1.00 78.21 D N

ATOM10180CA GLUD 349-12.391-18.369-9.291 1.00 79.65 D C

ATOM10181CB GLUD 349-11.289-17.343-9.558 1.00 50.17 D C

ATOM10182CG GLUD 349-11.372-16.611-10.8791.00 81.36 D C

ATOM 10183CD GLUD 349-10.282-15.560-11.0041.00 81.83 D C

ATOM 10184OE 1 D 349-10.083-14.804-10.0281.00 82.05 D O
GLU

ATOM 10185OE2GLUD 349-9.630 -15.486-12.0691.00 81.54 D O

ATOM 10186C GLUD 349-12.181-18.940-7.8951.00 80.27 D C

ATOM 10187O GLUD 349-11.961-20.136-7.7261.00 80.25 D O

ATOM 10188N ARGD 350-12.248-1_8.061-6.9001.00 81.38 D N

ATOM 10189CA ARGD 350-12.074-18.441-5.5011.00 82.12 D C

ATOM 10190CB ARGD 350-12.054-17.194-4.6131.00 81.91 D C

ATOM 10191CG ARGD 350-11.010-16.158-4.9661.00 81.59 D C

ATOM 10192CD ARGD 350-11.308-14.872-4.2221.0D 81.33 D C

ATOM 10193NE ARGD 350-10.335-13.819-4.4891.00 81.62 D N

ATOM 10194CZ ARGD 350-9.153 -13.715-3.8901.00 81.77 D C

ATOM 10195NH1ARGD 350-8.782 -14.604-2.9761.00 81.58 D N

ATOM 10196NH2ARGD 350-8.345 -12.710-4.2001.00 82.25 D N

ATOM 10197C ARGD 350-13.228-19.332-5.0561.00 82.78 D C

ATOM 10198O ARGD 350-13.325-19.703-3.8841.00 82.69 D O

ATOM 10199N GLYD 351-14.107-19.667-5.9951.00 83.53 D N

ATOM 10200CA GLYD 351-15.246-20.491-5.6561.00 84.18 D C

ATOM 10201C GLYD 351-16:133-19.737-4.6871.00 84.96 D C

ATOM 10202O GLYD 351-16.138-20.012-3.4881.00 84.92 D O

ATOM 10203N METD 352-16.870-18.763-5.2111.00 85.83 D N

ATOM 10204CA METD 352-17.779-17.962-4.4021.00 86.70 D C

ATOM 10205CB METD 352-17.156-16:601-4.0751.00 87.13 D C

ATOM 10206CG MET1 352-15.902-16.650-3.2171.00 87.70 D C
D

ATOM 10207SD METD 352-15.256-14.992-2.8631.00 88.29 D S

ATOM 10208CE METD 352-16.327-14.485-1.5201.00 88.11 D C

ATOM 10209C METD 352-19.085-17.741-5.1551.00 87.22 D C

ATOM 10210O METD 352-19.177-17.989-6.3601.00 87.18 D 0 ATOM 10211N GLUD 353-20.097-17.274-4.4341.00 88.02 D N

ATOM 10212CA GLUD 353-21.395-16.995-5.0351.00 88.47 D C

ATOM 10213CB GLUD 353-22.461-16.885-3.9431.00 89.61 D C

ATOM 10214CG GLUD 353-23.849-16.517-4.4411.00 90.97 D C

ATOM 10215CD GLUD 353-24.523-16.273-3.2991.00 92.07 D C

ATOM 10216OE1GLUD 353-25.064-17.214-2.5061.00 92.29 D O

ATOM 10217OE2GLUD 353-25.342-15.139-3.1941.00 92.22 D O

ATOM 10218C GLUD 353-21.272-15.666-5.7691.00 88.07 D C

ATOM 10219O GLUD 353-20.957-14.644-5.1561.00 85.00 D O

ATOM 10220N ILED 354-21.503-15.677-7.0781.00 87.01 D N

ATOM 10221CA ILED 354-21.403-14.450-7.8591.00 86.19 D C

ATOM 10222CB ILED 354-21.659-14.715-9.3581.00 86.14 D C

ATOM 10223CG2ILED 354-21.764-13.397-10.1111.00 86.52 D C

ATOM 10224CG1ILED 354-20.525-15.565-9.9381.00 86.02 D C

ATOM 10225CD1ILED 354-20.678-15.874-11.4171.00 85.51 D C

ATOM 10226C ILED 354-22.396-13.398-7.3621.00 85.71 D C

ATOM 10227O ILED 354-23.575-13.689-7.1581.00 86.15 D O

ATOM 10228N SERD 355-21,905-12.176-7.1661.00 84.48 D N

ATOM 10229CA SERD 355-22.745-11.076-6.6971.00 83.27 D C

ATOM 10230CB SERD 355-21.865-9.947-6.1461.00 83.11 D C

ATOM 10231OG SERD 355-21.117-10.366-5.0181.00 81.98 D O

ATOM 10232C SERD 355-23.625-10.536-7.8291.00 82.73 D C
ATOM 10233O SERD 355-23.324-10.731-9.0081.00 82.62 D O
ATOM 10234N PROD 356-24.731-9.851-7.4811.00 82.21 D N

ATOM 10235CD PROD 356-25.231-9.621-6.1131.00 82.00 D C
ATOM 10236CA PROD 356-25.654-9.280-8.4711.00 81.79 D C
ATOM 10237CB PROD 356-26.614-8.463-7.6101.00 81.54 D C

ATOM 10238CG PROD 356-26.683-9.257-6.3541.00 81.68 D C
ATOM 10239C PROD 356-24.952-8.416-9.5231.00 81.34 D C
ATOM 10240O PROD 356-24.045-7.644-9.2001.00 81.31 D O
ATOM 10241N METD 357-25.375-8.553-10.7771.00 80.82 D N
ATOM 10242CA METD 357-24.806-7.752-11.8841.00 80.36 D C
ATOM 10243CB METD 357-24.954-6.251-11.6271.00 80.44 D C
ATOM 10244CG METD 357-26.374-5.775-11.5561.00 50.44 D C
ATOM 10245SD METD 357-26.409x.073 -10.9781.00 80.50 D S
ATOM 10246CE METD 357-26.606-4.335-9.1941.00 80.02 D C
ATOM 10247C METD 357-23.335-8.066-12.1431.00 79.92 D C
ATOM 10248O METD 357-22.688-7.320-12.8781.00 80.41 D O
ATOM 10249N CYSD 358-22.800-9.130-11.5521.00 79.00 D N
ATOM 10250CA CYSD 358-21.390-9.447-11.7411.00 78.17 D C
ATOM 10251CB CYSD 358-20.717-9.651-10.3811.00 77,31 D C
ATOM 10252SG CYSD 358-20.755-8.191-9.3071.00 74.60 D S
ATOM 10253C CYSD 358-21.128-10.658-12.6341.00 78.45 D C
ATOM 10254O CYSD 358-19.972-10.98112.9171.00 78,28 D 0 ATOM 10255N ASPD 359-22.195-11.316-13.0851.00 78.54 D N
ATOM 10256CA ASPD 359-22.068-12.496-13.9431.00 78.65 D C
ATOM 10257CB ASPD 359-23.221-13.464-13.6681.00 78.46 D C
ATOM 10258CG ASPD 359-22.960-14.857-14.2131.00 78.80 D C
ATOM 10259OD1ASPD 359-22.615-14.984-15.4091.00 78.37 D O
ATOM 10260OD2ASPD 359-23.106-15.828-13.4411.00 78.73 D 0 ATOM 10261C ASPD 359-22.069-12.096-15.4211,00 78.66 D C
ATOM 10262O ASPD 359-23.127-11.823-15.9931.00 78.41 D O
ATOM 10263N LYSD 360-20.889-12.078-16.0391.00 78.95 D N
ATOM 10264CA LYS0 360-20.765-11.688-17.4451.00 79.77 D C
ATOM 10265CB LYSD 360-19.310-11.350-17.7911.00 79.01 D C
ATOM 10266CG LYSD 360-15.381-12.552-17:8781.00 78.58 D C
ATOM 10267CD LYSD 360-17.004-12.140-18.3831.00 77.48 D C
ATOM 10268CE LYSD 360-16.039-13.311-18.3911,00 76.85 D C

ATOM10269NZ LYS D 360-14.696_-12.919-18.8991.00 75.62 D N

ATOM10270C LYS D 360-21.272-12.722-18.4411.00 80.47 D C

ATOM10271O LYS D 360-20.998-12.612-19.6361.00 80.87 D O

ATOM10272N HIS D 361-21.994-13.728-17.9541.00 81.15 D N

ATOM10273CA HIS D 361-22.545-14.769-18.8251.00 81.76 D C

ATOM10274GB HIS D 361-22.156-16.161-18.3151.00 81.93 D C

ATOM10275CG HIS D 361-20.678-16.415-18.3081.00 82.60 D C

ATOM10276CD2HIS D 361-19.832-16.740-17.2991.00 82.36 D C

ATOM10277ND1HIS D 361-19.906-16.354-19.4491.00 82.27 D N

ATOM10278CE1HIS D 361-18.650-16.632-19.1451.00 82.23 D C

ATOM10279NE2HIS D 361-18.579-16.871-17.8471.00 82.42 D N

ATOM10280C HIS D 361-24.064-14.621-18.8361.00 81.95 D C

ATOM10281O HIS D 361-24.735-14.952-19.8191.00 81.95 D O
i ATOM10282N ASN D 362-24.591-14.119-17.7231.00 81.88 D N
'' ATOM10283CA ASN D 362-26.020-13.882-17.5551.00 81.50 D C
I

ATOM10284CB ASN D 362-26.594-14.819-16.4861.00 82.24 D C

ATOM10285CG ASN D 362-26.545-16.280-16.9061.00 83.18 D C

ATOM10286OD1ASN D 362-27.133-16.668-17.9211.00 83.42 D O

ATOM10287ND2ASN D 362-25.842-17.099-16.1271.00 83.33 D N

ATOM10288C ASN D 362-26.172-12.426-17.1251.00 80.50 D C

ATOM10289O ASN D 362-26.630-12.130-16.0191.00 80.76 D O

ATOM10290N ALA D 363-25.776-11.524-18.0191.00 78.88 D N

ATOM10291CA ALA D 363-25.827-10.094-17.7521.00 76.75 D C

ATOM10292CB ALA D 363-24.515-9.449-18.1841.00 76.83 D C

ATOM10293C ALA D 363-26.995-9.375-18.4121.00 75.07 D C

ATOM10294O ALA D 363-27.154-9.407-19.6291.00 75.64 D O

ATOM10295N SER D 364-27.805_-8.721-17.5901.00 73.05 D N

ATOM10296CA SER D 364-28.948-7.959-18.0621.00 71.03 D C

ATOM10297CB SER D 364-30.191-8.332-17.2551.00 71.40 D C

ATOM10298OG SER D 364-30.327-9.738-17.1581.00 71.83 D O

ATOM10299C SER D 364-28.594-6.493-17.8261.00 69.52 D C

ATOM10300O SER D 364-29.273-5.792-17.0821.00 68.88 D O

ATOM10301N VAL D 365-27.516-6.041-18.4581.00 67.97 D N

ATOM10302CA VAL D 365-27.051-4.668-18.3001.00 66.62 D C

ATOM10303CB VAL D 365-25.937-4.328-19.3141.00 66.28 D C

ATOM10304CG1VAL D 365-25.576-2.851-19.2111.00 65.30 D C

ATOM10305CG2VAL D 365-24.706-5.193-19.0441.00 65.71 D C

ATOM10306C VAL D 365-28.149-3.622-18.4261.00 66.00 D C

ATOM10307O VAL D 365-28.399-2.867-17.4821.00 66.14 D O

ATOM10308N GLU D 366-28.801-3.564-19.5851.00 65.00 D N

ATOM10309CA GLU D 366-29.859-2.582-19.7851.00 63.79 D C

ATOM10310CB GLU D 366-30.490-2.730-21.1721.00 64.29 D C

ATOM10311CG GLU D 366-29.520-2.610-22.3381.00 63.75 D C

ATOM10312CD GLU D 366-28.677-3.858-22.5221.00 64.10 D C

ATOM10313OE1GLU D 366-28.970-4.868-21.8441.00 63.99 D O

ATOM10314OE2GLU D 366-27.733-3.832-23.3481.00 63.22 D O

ATOM10315C GLU D 366-30.929-2.747-18.7111.00 62.89 D C

ATOM10316O GLU D 366-31.372-1.770-18.1061.00 63.16 D O

ATOM10317N LYS D 367-31.331-3.989-18.4691.00 61.66 D N

ATOM10318CA LYS D 367-32.341-4.279-17.4631.00 60.41 D C

ATOM10319CB LYS D 367-32.597-5.789-17.3991.00 62.79 D C

ATOM10320CG LYS D 367-33.710-6.199-16.4391.00 65.99 D C

ATOM10321CD LYS D 367-33.905-7.717-16.4181.00 69.04 D C

ATOM10322CE LYS D 367-34.932-8.140-15.3591.00 70.74 D C

ATOM10323NZ LYS D 367.-35.181-9.621-15.3381.00 71.57 D N

ATOM10324C LYS D 367-31.889-3.759-16.1011.00 58.14 D C

ATOM103250 LYS D 367-32.690-3.223-15.3361.00 58.33 D O

ATOM10326N SER D 368-30.601-3.915-15.8061.00 55.84 D N

ATOM10327CA SER D 368-30.036x.454 -14.5401.00 53.16 D C

ATOM10328CB SER D 368-28.569-3.856-14.4351.00 53.13 D C

ATOM10329OG 5ER D 368-28.457-5.246-14.1981.00 55.33 D O

ATOM10330C SER D 368-30.152-1.948-14.3711.00 50.89 D C

ATOM10331O SER D 368-30.570-1.463-13.3201.00 49.17 D O

ATOM10332N GLN D 369-29.774-1.206-15.4031.00 48.53 D N

ATOM10333CA GLN D 369-29.8620.239 -15.3191.00 46.99 D C

ATOM10334CB GLN D 369-29.3850.888 -16.6201.00 46.19 D C

ATOM10335CG GLN D 369-27.8840.765 -16.7981.00 45.52 D C

ATOM10336CD GLN D 369-27.1351.165 -15.5291.00 46.37 D C

ATOM10337OE1GLN D 369-27.1442.337 -15.1311.00 44.91 D 0 ATOM10338NE2GLN D 369-26.5040.188 -14.8761.00 43.88 D N

ATOM10339C GLN D 369-31.2930.624 -15.0081.00 46.69 D C

ATOM103400 GLN D 369-31.5441.441 _ -14.1171.00 46.61 D O

ATOM10341N VAL D 370-32.2330.010 -15.7231.00 45.72 D N

ATOM10342CA VAL D 370-33.6470.289 -15.5111.0D 44.54 D C

ATOM10343CB VAL D 370-34.535-0.593-16.4261.00 45.47 D C

ATOM10344CG1VAL D 370-36.014-0.287-16.1781.0D 44.58 D C

ATOM10345CG2VAL D 370-34.179-0.341-17.8911.00 44.07 D C

ATOM10346C VAL D 370-33.9980.032 -14.0491.00 44.18 D C

ATOM10347O VAL D 370-34.7000.829 -13.4201.00 44.76 D O

ATOM10348N GLY D 371-33.496-1.074-13.5041.00 42.96 D N

ATOM10349CA GLY D 371-33.767-1.388-12.1141.00 42.57 D C

ATOM10350C GLY D 371-33.138-0.380-11.1661.00 43.00 D C

ATOM10351O GLY D 371-33.7960.099 -10.2411.00 43.55 D O

ATOM10352N PHE D 372-31.867-0.053-11.4011.00 43.30 D N
ATOM10353CA PHE D 372-31.1290.902 -10.5651.00 43.58 D C

ATOM10354CB PHE D 372-29.6771.031 -11.0621.00 43.24 D C

DE~I~.NI3ES OU BRE'~ETS 'VOLUNI~NEUX
LA PRESENTS P:~RTIE DE CETTE DEi~L~NDE OU CE BI~.EVETS
COVIPREND PLUS D'U~I TOME.
CECI EST LE TOIVIE ~ D
NOTE: Pour les tomes additionels, veillez contacter 1e Bureau Canadien des Brevets.
~1VIB~ APPLICAT~~N~ / P~-TENTS
THIS SECTION OF THE APPLiCfi T IuiV l Poi T EN T CON T fins ~iO~E
TH~1.N ONE VOLUl~IE.
THIS IS VOLUI~IE ~ OF
NOTE: For additional volumes please contact the Canadian Patent Office.

Claims (110)

What is claimed is:

1. A crystalline form comprising a substantially pure phosphodiesterase 4D2 (PDE4D2) polypeptide.

2. A crystalline form comprising a substantially pure phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide in complex with a ligand.

3. The crystalline form of claim 2, wherein the crystalline form has unit cell a = 99.2 .ANG.; b = 111.2 .ANG.; c = 159.7 .ANG..

4. The crystalline form of claim 2, wherein the crystalline form has a space group of P2 1 2 1 2 1. ~

5. The crystalline form of claim 2, wherein the crystalline form comprises four phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptides.

6. The crystalline form of claim 2, wherein the crystalline form is such that the three-dimensional structure of the crystallized complex can be determined to a resolution of about 2.3 .ANG. or better.

7. The crystalline form of claim 2, wherein the phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide teas the amino acid sequence shown in SEQ ID NO:4.

8. The crystalline form of claim 2, wherein the complex has a crystalline structure further characterized by the coordinates corresponding to one of Table 4 and Table 5.

9. A method of generating a crystalline form comprising a phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide in complex with a ligand, the method comprising:

a) incubating a solution comprising a phosphodiesterase 4D2 (PDE4D2) catalytic domain and a ligand; and b) crystallizing the phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide and ligand by vapor diffusion, whereby a crystalline form of a phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide in complex with a ligand is generated.

10. The method of claim 9, wherein the crystalline form is grown by vapor diffusion against a well buffer comprising 50 mM HEPES (pH 7.5), 15% PEG3350, 25% ethylene glycol, 5% methanol, and 5% DMSO.

11. The method of claim 10, wherein the crystalline form is grown at 4°C.

12. The method of claim 9, wherein the ligand is cAMP.

13. The method of claim 12, wherein the solution comprises 10 mM
cAMP, 0.4 mM zinc sulfate, 15 mg/mL phosphodiesterase 4D2 (PDE4D2) in a storage buffer of 50 mM NaCI, 20 mM Tris-HCI (pH 7.5), and 1 mM .beta.-mercaptoethanol.

14. The method of claim 12, further comprising saturating cAMP
binding by soaking the crystalline form in a buffer of 50 mM HEPES (pH 7.5), 20% PEG3350, 25% ethylene glycol, 0.4 mM zinc sulfate, and 50 mM cAMP.

15. The method of claim 14, wherein the saturating occurs at room temperature.

16. A crystalline form formed by the method of claim 8.

17.A binding site in a human phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide for a substrate, wherein the substrate is in van der Waals, hydrogen bonding, or both van der Waals and hydrogen bonding contact with at least one of the following residues of the human phosphodiesterase 4D2 (PDE4D2) polypeptide: Tyr159, His160, His164, His200, Asp201, Met273, Asp318, Leu319, Asn321, Thr333, I1e336, Phe340, GIn369, and Phe372.

18. The binding site of claim 17, comprising four phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptides.

19. The binding site of claim 18, wherein at least two of the four phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptides are in van der Waals, hydrogen bonding, or both van der Waals and hydrogen banding contact through at least one of the following residues: Arg116, Met147, Thr148, Asp151, Asn214, Thr215, Asn216, G1u218, A1a220; Leu221, Met222, Tyr223, Asn224, Asp225, Asn231, Leu234, A1a235, Lys239, GIn242, GIu243, GIu244, Lys254, Arg257, GIn2 58, Arg261, Ile265, Arg346, Glu349, and Arg350.

20. The binding site of claim 17, further comprising a metal ion.

21. A complex of a human phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide and a substrate, wherein the substrate is in van der Waals, hydrogen bonding, or both van der Waals and hydrogen bonding contact with at least one of the following residues of the human phosphodiesterase 4D2 (PDE4D2) polypeptide: Tyr159, His160, His164, His200, Asp201, Met273, Asp318, Leu319, Asn321, Thr333, Ile336, Phe340, Gln369, and Phe372.

22. The complex of claim 21, comprising four phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptides.

23. The complex of claim 22, wherein at least two of the four phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptides are in van der Waals, hydrogen bonding, or both van der Waal and hydrogen bonding contact through one or more of the following residues: Arg116, Met147, Thr148, Asp151, Asn214, Thr215, Asn216, Glu218, Ala220, Leu221, Met222, Tyr223, Asn224, Asp225, Asn231, Leu234, Ala235, Lys239, Gln242, Glu243, Glu244, Lys254, Arg257, Gln258, Arg261, Ile265, Arg346, Glu349, and Arg350.

24. The complex of claim 21, further comprising a metal ion.

25. A crystal of the complex of claim 21.

26. The crystal of claim 25, having the following physical measurements: space group P2 1 2 1 2 1; and unit cell a = 99.2 .ANG.; b =
111.2 .ANG.;
c = 159.7 .ANG..

27. A method for identifying a phosphodiesterase ligand, the method comprising:
a) providing atomic coordinates of a phosphodiesterase 4D2 (PDE4D2) catalytic domain in complex with a ligand to a computerized modeling system; and b) modeling a ligand that fits spatially into the binding site of the phosphodiesterase 4D2 (PDE4D2) catalytic domain to thereby identify a phosphodiesterase ligand.

28. The method of claim 27, wherein the phosphodiesterase 4D2 (PDE4D2) catalytic domain comprises the amino acid sequence of SEQ ID
NO:4.

29. The method of claim 27, wherein the method further comprises identifying in an assay for phosphodiesterase-mediated activity a modeled ligand that increases or decreases the activity of the phosphodiesterase.

30. The method of claim 27, wherein the phosphodiesterase is PDE4D2.

31. A method of identifying a phosphodiesterase 4D2 (PDE4D2) ligand that selectively binds a phosphodiesterase 4D2 (PDE4D2) polypeptide compared to other polypeptides, the method comprising:
a) providing atomic coordinates of a phosphodiesterase 4D2 (PDE4D2) catalytic domain in complex with a ligand to a computerized modeling system; and b) modeling a ligand that fits into the binding pocket of a phosphodiesterase 4D2 (PDE4D2) catalytic domain and that interacts with residues of a phosphodiesterase 4D2 (PDE4D2) catalytic domain that are conserved among phosphodiesterase 4D2 (PDE4D2) subtypes to thereby identify a phosphodiesterase 4D2 (PDE4D2) ligand that selectively binds a phosphodiesterase 4D2 (PDE4D2) polypeptide compared to other polypeptides.

32. The method of claim 31, wherein the phosphodiesterase 4D2 (PDE4D2) catalytic domain comprises the amino acid sequence shown in SEQ ID NO:4.

33. The method of claim 31, further comprising identifying in a biological assay for phosphodiesterase 4D2 (PDE4D2) activity a modeled ligand that selectively binds to said phosphodiesterase 4D2 (PDE4D2) and increases or decreases the activity of the phosphodiesterase 4D2 (PDE4D2).

34. A method for designing a ligand of a phosphodiesterase 4D2 (PDE4D2) polypeptide, the method comprising:

a) forming a complex of a compound bound to the phosphodiesterase 4D2 (PDE4D2) polypeptide;
b) determining a structural feature of the complex formed in (a);
wherein the structural feature is of a binding site for the compound; and c) using the structural feature determined in (b) to design a ligand of a phosphodiesterase 4D2 (PDE4D2) polypeptide capable of binding to the binding site of claim 16.

35. The method of claim 33, further comprising using a computer-based model of the complex formed in (a) in designing the ligand.

36. A method of designing a ligand of a phosphodiesterase polypeptide, the method comprising:
a) selecting a candidate phosphodiesterase ligand;
b) determining which amino acid or amino acids of a phosphodiesterase polypeptide interact with the ligand using a three-dimensional model of a crystallized protein, the model comprising a phosphodiesterase 4D2 (PDE4D2) catalytic domain in complex with a ligand;
c) identifying in a biological assay for phosphodiesterase activity a degree to which the ligand modulates the activity of the phosphodiesterase polypeptide;
d) selecting a chemical modification of the ligand wherein the interaction between the amino acids of the phosphodiesterase polypeptide and the ligand is predicted to be modulated by the chemical modification;
e) synthesizing a ligand having the chemical modified to form a modified ligand;
f) contacting the modified ligand with the phosphodiesterase polypeptide;
g) identifying in a biological assay for phosphodiesterase activity a degree to which the modified ligand modulates the biological activity of the phosphodiesterase polypeptide; and h) comparing the biological activity of the phosphodiesterase polypeptide in the presence of modified ligand with the biological activity of the phosphodiesterase polypeptide in the presence of the unmodified ligand, whereby a ligand of a phosphodiesterase polypeptide is designed.

37. The method of claim 36, wherein the phosphodiesterase is phosphodiesterase 4D2 (PDE4D2)

38. The method of claim 37, wherein the phosphodiesterase 4D2 (PDE4D2) polypeptide is a human phosphodiesterase 4D2 (PDE4D2) polypeptide.

39. The method of claim 37, wherein the phosphodiesterase 4D2 (PDE4D2) polypeptide comprises the amino acid sequence of SEQ ID NO:4.

40.The method of claim 36, further comprising repeating steps (a) through (f), if the biological activity of the phosphodiesterase polypeptide in the presence of the modified ligand varies from the biological activity of the phosphodiesterase polypeptide in the presence of the unmodified ligand.

41. A method of designing a chemical compound that modulates the biological activity of a target phosphodiesterase polypeptide, the method comprising:
a) obtaining three-dimensional structures for a catalytic domain (CD) of phosphodiesterase 4D2 (PDE4D2) bound to a ligand, wherein the structures are selected from the group consisting of X-ray structures and computer generated models;
b) rotating and translating the three-dimensional structures as rigid bodies so as to superimpose corresponding backbone atoms of a core region of the phosphodiesterase 4D2 (PDE4D2) CD;
c) comparing the superimposed three-dimensional structures to identify volume near a catalytic pocket of the PDE CD that is available to a ligand in one or more structures, but not available to the ligand in one or more other structures;
d) designing a chemical compound that could occupy the volume in some of the complexed structures, but not in others;

e) synthesizing the designed chemical compound; and f) testing the designed chemical compound in a biological assay to determine whether it acts as a ligand of a phosphodiesterase with a desired effect on phosphodiesterase biological activities, whereby a ligand of a phosphodiesterase polypeptide is designed.

42. The method of claim 41, further comprising designing a chemical compound by considering a known ligand of the PDE CD and adding a substituent that protrudes into the volume identified in step (c) or that makes a desired interaction.

43. The method of claim 41, wherein the phosphodiesterase is PDE4D2.

44. The method of any one of claims 41-43, wherein the designing a chemical compound further comprises using computer modeling software.

45. A method of designing a ligand that selectively modulates the activity of a phosphodiesterase polypeptide, the method comprising:
a) evaluating a three-dimensional structure of a crystallized phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide in complex with a ligand; and b) synthesizing a potential ligand based on the three-dimensional structure of the crystallized phosphodiesterase 4D2 (PDE4D2) catalytic polypeptide in complex with a ligand, whereby a ligand that selectively modulates the activity of a phosphodiesterase polypeptide is designed.

46. The method of claim 45, wherein the phosphodiesterase is phosphodiesterase 4D2 (PDE4D2).

47. The method of claim 46, wherein the phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide comprises the amino acid sequence of SEQ ID NO:4.

48. The method of claim 45, wherein the crystallized phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide is in an orthorhombic crystalline form.

49. The method of claim 48, wherein the three-dimensional structure of the crystallized phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide in complex with a ligand can be determined to a resolution of about 2.3 .ANG. or better.

50. The method of claim 45, wherein the method further comprises contacting a phosphodiesterase catalytic domain polypeptide with the potential ligand and a ligand; and assaying the phosphodiesterase catalytic domain polypeptide for binding of the potential ligand, for a change in activity of the phosphodiesterase catalytic domain polypeptide, or both.

51. A method of screening a plurality of compounds for a ligand of a phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide, the method comprising:
a) providing a library of test samples;
b) contacting a crystalline form comprising a phosphodiesterase 4D2 (PDE4D2) polypeptide in complex with a ligand with each test sample;
c) detecting an interaction between a test sample and the crystalline phosphodiesterase 4D2 (PDE4D2) polypeptide in complex with a ligand;
d) identifying a test sample that interacts with the crystalline phosphodiesterase 4D2 (PDE4D2) polypeptide in complex with a ligand; and e) isolating a test sample that interacts with the crystalline phosphodiesterase 4D2 (PDE4D2) polypeptide in complex with a ligand, whereby a plurality of compounds is screened for a ligand of a phosphodiesterase 4D2 (PDE4D2) catalytic domain polypeptide.

52. The method of claim 51, wherein the phosphodiesterase 4D2 (PDE4D2) polypeptide comprises a phosphodiesterase 4D2 (PDE4D2) catalytic domain.

53. The method of claim 51, wherein the phosphodiesterase 4D2 (PDE4D2) polypeptide is a human phosphodiesterase 4D2 (PDE4D2) polypeptide.

54. The method of claim 53, wherein the phosphodiesterase 4D2 (PDE4D2) polypeptide comprises the amino acid sequence of SEQ ID NO:4.

55. The method of claim 51, wherein the library of test samples are bound to a substrate.

56. The method of claim 51, wherein the library of test samples are synthesized directly on a substrate.

57. A crystallized, recombinant polypeptide comprising: (a) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (b) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (c) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID
NO: 3 and has at least one biological activity of PDE4D2; wherein the polypeptide of (a), (b) or (c) is in crystal form.

58. A crystallized complex comprising the crystallized, recombinant polypeptide of claim 57 and a co-factor, wherein the complex is in crystal form.

59. A crystallized complex comprising the crystallized, recombinant polypeptide of claim 57 and a small organic molecule, wherein the complex is in crystal form.

60. The crystallized, recombinant polypeptide of claim 57, which diffracts x-rays to a resolution of about 3.5 .ANG. or better.

61. The crystallized, recombinant polypeptide of claim 57, wherein the polypeptide comprises at least one heavy atom label.

62. The crystallized, recombinant polypeptide of claim 61, wherein the polypeptide is labeled with seleno-methionine.

63. A method for designing a modulator for the prevention or treatment of a disease or disorder, comprising:
a) providing a three-dimensional structure for a crystallized, recombinant polypeptide of claim 1;
b) identifying a potential modulator for the prevention or treatment of a disease or disorder by reference to the three-dimensional structure;

c) contacting a polypeptide of the composition of claim 1 or a phosphodiesterase (PDE) with the potential modulator; and d) assaying the activity of the polypeptide after contact with the modulator, wherein a change in the activity of the polypeptide indicates that the modulator may be useful for prevention or treatment of a disease or disorder.

64. A method for obtaining structural information of a crystallized polypeptide, the method comprising:
a) crystallizing a recombinant polypeptide, wherein the polypeptide comprises: (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID
NO: 3 and has at least one biological activity of human PDE4D2; and wherein the crystallized polypeptide is capable of diffracting X-rays to a resolution of 3.5 .ANG. or better; and b) analyzing the crystallized polypeptide by X-ray diffraction to determine the three-dimensional structure of at least a portion of the crystallized polypeptide.

65. The method of claim 64, wherein the three-dimensional structure of the portion of the crystallized polypeptide is determined to a resolution of 3.5 .ANG. or better.

66. A method for identifying a druggable region of a polypeptide, the method comprising:
a) obtaining crystals of a polypeptide comprising (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO:
1 or SEQ ID NO: 3 and has at least one biological activity of human PDE4D2, such that the three dimensional structure of the crystallized polypeptide may be determined to a resolution of 3.5 .ANG. or better;
b) determining the three dimensional structure of the crystallized polypeptide using X-ray diffraction; and c) identifying a druggable region of the crystallized polypeptide based on the three-dimensional structure of the crystallized polypeptide.

67. The method of claim 66, wherein the druggable region is an active site.

68. The method of claim 67, wherein the druggable region is on the surface of the polypeptide.

69. 13. Crystalline human PDE4D2 comprising a crystal having unit cell dimensions a = 99.2 .ANG.; b = 111.2 .ANG.; c = 159.7 .ANG., .alpha. =
.beta. = .gamma. = 90°, with an orthorhombic space group P2 1 2 1 2 1 and 4 molecules per asymmetric unit.

70. A crystallized polypeptide comprising (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID
NO: 3 and has at least one biological activity of human PDE4D2; wherein the crystal has a P2 1 2 1 2 1 space group.

71. A crystallized polypeptide comprising a structure of a polypeptide that is defined by a substantial portion of the atomic coordinates set forth in Table 4 or Table 5.

72. A method for determining the crystal structure of a homolog of a polypeptide, the method comprising:
a) providing the three dimensional structure of a first crystallized polypeptide comprising (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID
NO: 3 and has at least one biological activity of human PDE4D2;
b) obtaining crystals of a second polypeptide comprising an amino acid sequence that is at least 70% identical to the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4, such that the three dimensional structure of the second crystallized polypeptide may be determined to a resolution of 3.5 .ANG. or better; and c) determining the three dimensional structure of the second crystallized polypeptide by x-ray crystallography based on the atomic coordinates of the three dimensional structure provided in step (a).

73. The method of claim 72, wherein the atomic coordinates for the second crystallized polypeptide have a root mean square deviation from the backbone atoms of the first polypeptide of not more than 1.5 .ANG. for all backbone atoms shared in common with the first polypeptide and the second polypeptide.

74. A method for homology modeling a homolog of human PDE4D2, comprising:
a) aligning the amino acid sequence of a homolog of human PDE4D2 with an amino acid sequence of SEQ ID NO: 2 or SEQ ID NO: 4 and incorporating the sequence of the homolog of human PDE4D2 into a model of human PDE4D2 derived from structure coordinates as listed in Table 4 or Table 5 to yield a preliminary model of the homolog of human PDE4D2;
b) (b) subjecting the preliminary model to energy minimization to yield an energy minimized model;

c) (c) remodeling regions of the energy minimized model where stereochemistry restraints are violated to yield a final model of the homolog of human PDE4D2.

75. A method for obtaining structural information about a molecule or a molecular complex of unknown structure comprising:

a) crystallizing the molecule or molecular complex;

b) generating an x-ray diffraction pattern from the crystallized molecule or molecular complex;

c) applying at least a portion of the structure coordinates set forth in Table 4 or Table 5 to the x-ray diffraction pattern to generate a three-dimensional electron density map of at least a portion of the molecule or molecular, complex whose structure is unknown.

76. A method for attempting to make a crystallized complex comprising a polypeptide and a modulator having a molecular weight of less than 5 kDa, the method comprising:

a) crystallizing a polypeptide comprising (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID
NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO:
1 or SEQ ID NO: 3 and has at least one biological activity of human PDE4D2; such that crystals of the crystallized polypeptide will diffract x-rays to a resolution of 5 .ANG. or better;
and b) soaking the crystals in a solution comprising a potential modulator having a molecular weight of less than 5 kDa.

77. A method for incorporating a potential modulator in a crystal of a polypeptide, comprising placing a hexagonal crystal of human PDE4D2 having unit cell dimensions a = 99.2 .ANG.; b = 111.2 .ANG.; c = 159.7 .ANG., .alpha. = .beta. = .gamma. =

90°, with an orthorhombic space group P2 1 2 1 2 1, in a solution comprising the potential modulator.

78. A computer readable storage medium comprising digitally encoded structural data, wherein the data comprises structural coordinates as listed in Table 4 or Table 5 for the backbone atoms of at least about six amino acid residues from a druggable region of human PDE4D2.

79. A scalable three-dimensional configuration of points, at least a portion of the points derived from some or all of the structure coordinates as listed in Table 4 or Table 5 for a plurality of amino acid residues from a druggable region of human PDE4D2.

80. The scalable three-dimensional configuration of points of claim 79, wherein the structure coordinates as listed in Table 4 or Table 5 for the backbone atoms of at least about five amino acid residues from a druggable region of human PDE4D2 are used to derive part or all of the portion of points.

81. The scalable three-dimensional configuration of points of claim 79, wherein the structure coordinates as listed in Table 4 or Table 5 for the backbone and optionally the side chain atoms of at least about ten amino acid residues from a druggable region of human PDE4D2 are used to derive part or all of the portion of points.

82. The scalable three-dimensional configuration of points of claim 79, wherein the structure coordinates as listed in Table 4 or Table 5 for the backbone atoms of at least about fifteen amino acid residues from a druggable region of human PDE4D2 are used to derive part or all of the portion of points.

83. The scalable three-dimensional configuration of points of claim 79, wherein substantially all of the points are derived from structure coordinates as listed in Table 4 or Table 5.

84. The scalable three-dimensional configuration of points of claim 79, wherein the structure coordinates as listed in Table 4 or Table 5 for the atoms of the amino acid residues from any of the above-described druggable regions of human PDE4D2 are used to derive part or all of the portion of points.

85. A scalable three-dimensional configuration of points, comprising points having a root mean square deviation of less than about 1.5 A from the three dimensional coordinates as listed in Table 4 or Table 5 for the backbone atoms of at feast five amino acid residues, wherein the five amino acid residues are from a druggable region of human PDE4D2.

86. The scalable three-dimensions! configuration of points of claim 85, wherein any point-to-point distance, calculated from the three dimensional coordinates as listed in Table 4 or Table 5, between one of the backbone atoms for one of the five amino acid residues and another backbone atom of a different one of the five amino acid residues is not more than about 10 .ANG..

87. A scalable three-dimensional configuration of points comprising points having a root mean square deviation of less than about 1.5 A from the three dimensions! coordinates as listed in Table 4 or Table 5 for the atoms of the amino acid residues from any of the above-described druggable regions of human PDE4D2.

88. A computer readable storage medium comprising digitally encoded structural data, wherein the data comprise the identity and three-dimensional coordinates as listed in Table 4 or Table 5 for the atoms of the amino acid residues from any of the above-described druggable regions of human PDE4D2.

89. A scalable three-dimensional configuration of points, wherein the points have a root mean square deviation of less than about 1.5 A from the three dimensional coordinates as listed in Table 4 or Table 5 for the atoms of the amino acid residues from any of the above-described druggable regions of human PDE4D2, Wherein up to one amino acid residue in each of the regions may have a conservative substitution thereof.

90. A scalable three-dimensional configuration of points derived from a druggable region of a polypeptide, wherein the points have a root mean square deviation of less than about 1.5 A from the three dimensional coordinates as listed in Table 4 or Table 5 for the backbone atoms of at least ten amino acid residues that participate in the intersubunit contacts of human PDE4D2.

91. A computer-assisted method for identifying an inhibitor of the activity of human PDE4D2, comprising:

a) supplying a computer modeling application with a set of structure coordinates as listed in Table 4 or Table 5 for the atoms of the amino acid residues from any of the above-described druggable regions of human PDE4D2 so as to define part or all of a molecule or complex;

b) supplying the computer modeling application with a set of structure coordinates of a chemical entity; and c) determining whether the chemical entity is expected to bind to or interfere with the molecule or complex.

92. The method of claim 91, wherein determining whether the chemical entity is expected to bind to or interfere with the molecule or complex comprises performing a fitting operation between the chemical entity and a druggable region of the molecule or complex, followed by computationally analyzing the results of the fitting operation to quantify the association between the chemical entity and the druggable region.

93. The method of claim 91, further comprising screening a library of chemical entities.

94. A computer-assisted method for designing an inhibitor of PDE4D2 activity comprising:

a) supplying a computer modeling application with a set of structure coordinates having a root mean square deviation of less than about 1.5 .ANG. from the structure coordinates as listed in Table 4 or Table 5 for the atoms of the amino acid residues from any of the above-described druggable regions of human PDE4D2 so as to define part or all of a molecule or complex;
b) supplying the computer modeling application with a set of structure coordinates for a chemical entity;
c) evaluating the potential binding interactions between the chemical entity and the molecule or complex;
d) structurally modifying the chemical entity to yield a set of structure coordinates for a modified chemical entity; and e) determining whether the modified chemical entity is an inhibitor expected to bind to or interfere with the molecule or complex, wherein binding to or interfering with the molecule or molecular complex is indicative of potential inhibition of PDE4D2 activity.

95. The method of claim 94, wherein determining whether the modified chemical entity is an inhibitor expected to bind to or interfere with the molecule or complex comprises performing a fitting operation between the chemical entity and the molecule or complex, followed by computationally analyzing the results of the fitting operation to evaluate the association between the chemical entity and the molecule or complex.

96. The method of claim 94, wherein the set of structure coordinates for the chemical entity is obtained from a chemical library.

97. A computer-assisted method for designing an inhibitor of PDE4D2 activity de novo comprising:

a) supplying a computer modeling application with a set of three-dimensional coordinates derived from the structure coordinates as listed in Table 4 or Table 5 for the atoms of the amino acid residues from any of the above-described druggable regions of human PDE4D2 so as to define part or all of a molecule or complex;

b) computationally building a chemical entity represented by a set of structure coordinates; and c) determining whether the chemical entity is an inhibitor expected to bind to or interfere with the molecule or complex, wherein binding to or interfering with the molecule or complex is indicative of potential inhibition of PDE4D2 activity.

98. The method of claim 97, wherein determining whether the chemical entity is an inhibitor expected to bind to or interfere with the molecule or complex comprises performing a fitting operation between the chemical entity and a druggable region of the molecule or complex, followed by computationally analyzing the results of the fitting operation to quantify the association between the chemical entity and the druggable region.

99. The method of any of claims 91, 94 or 97, further comprising supplying or synthesizing the potential inhibitor, then assaying the potential inhibitor to determine whether it inhibits PDE4D2 activity.

100. A method for identifying a potential modulator for the prevention or treatment of a disease or disorder, the method comprising:

a) providing the three dimensional structure of a crystallized polypeptide comprising: (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID
NO: 3 and has at least one biological activity of human PDE4D2;

b) obtaining a potential modulator for the prevention or treatment of a disease or disorder based on the three dimensional structure of the crystallized polypeptide;

c) contacting the potential modulator with a second polypeptide comprising: (i) an amino acid sequence set forth in SEQ ID
NO: 2 or SEQ ID NO: 4; (ii) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (iii) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID NO: 3 and has at least one biological activity of human PDE4D2; which second polypeptide may optionally be the same as the crystallized polypeptide; and d) assaying the activity of the second polypeptide, wherein a change in the activity of the second polypeptide indicate s that the compound may be useful for prevention or treatment of a disease or disorder.

101. A method for designing a candidate modulator for screening for inhibitors of a polypeptide, the method comprising:

a) providing the three dimensional structure of a druggable region of a polypeptide comprising (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEC ID
NO: 1 or SEQ ID

NO: 3 and has at least one biological activity of human PDE4D2; and b) designing a candidate modulator based on the three dimensional structure of the druggable region of the polypeptide.

102. A method for identifying a potential modulator of a polypeptide from a database, the method comprising:

a) providing the three-dimensional coordinates for a plurality of the amino acids of a polypeptide comprising (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ
ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID
NO: 2 or SEQ ID

NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO:

1 or SEQ ID NO: 3 and has at least one biological activity of human PDE4D2;

b) identifying a druggable region of the polypeptide;
and c) selecting from a database at least one potential modulator comprising three dimensional coordinates which indicate that the modulator may bind or interfere with the druggable region.

103. The method of claim 102, wherein the modulator is a ,mall molecule.

104. A method for preparing a potential modulator of a druggable region contained in a polypeptide, the method comprising:

a) using the atomic coordinates for the backbone atoms of at feast about six amino acid residues from a polypeptide of SEQ
ID NO: 4, with a ~ a root mean square deviation from the backbone atoms of the amino acid residues of not more than 1.5 A, to generate one or more three-dimensional structures of a molecule comprising a druggable region from the polypeptide;

b) employing one or more of the three dimensional structures of the molecule to design or select a potential modulator of the druggable region; and c) synthesizing or obtaining the modulator.

105. An apparatus for determining whether a compound is a potential modulator of a polypeptide, the apparatus comprising:

a) a memory that comprises:

i) the three dimensional coordinates and identities of at least about fifteen atoms from a druggable region of a polypeptide comprising (1) an amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; (2) an amino acid sequence having at least about 95% identity with the amino acid sequence set forth in SEQ ID NO: 2 or SEQ ID NO: 4; or (3) an amino acid sequence encoded by a polynucleotide that hybridizes under stringent conditions to the complementary strand of a polynucleotide having SEQ ID NO: 1 or SEQ ID NO: 3 and has at least one biological activity of human PDE4D2;

ii) executable instructions; and b) a processor that is capable of executing instructions to:

i) receive three-dimensional structural information for a candidate modulator;

ii) determine if the three-dimensional structure of the candidate modulator is complementary to the three dimensional coordinates of the atoms from the druggable region; and iii) output the results of the determination.

106. A method for making an inhibitor of PDE4D2 activity, the method comprising chemically or enzymatically synthesizing a chemical entity to yield an inhibitor of PDE4D2 activity, the chemical entity having been identified during a computer-assisted process comprising supplying a computer modeling application with a set of structure coordinates of a molecule or complex, the molecule or complex comprising at least a portion of at least one druggable region from human PDE4D2; supplying the computer modeling application with a set of structure coordinates of a chemical entity; and determining whether the chemical entity is expected to bind or to interfere with the molecule or complex at a druggable region, wherein binding to or interfering with the molecule or complex is indicative of potential inhibition of PDE4D2 activity.

107. A computer readable storage medium comprising digitally encoded data, wherein the data comprises structural coordinates for a druggable region that is structurally homologous to the structure coordinates as listed in Table 4 or Table 5 for a druggable region of human PDE4D2.

108. A computer readable storage medium comprising digitally encoded structural data, wherein the data comprise a majority of the three-dimensional structure coordinates as listed in Table 4 or Table 5.

109. The computer readable storage medium of claim 52, further comprising the identity of the atoms for the majority of the three-dimensional structure coordinates as listed in Table 4 or Table 5.

110. The computer readable storage medium of claim 52, wherein the data comprise substantially all of the three-dimensional structure coordinates as listed in Table 4 or Table 5.